The Enzyme Database

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EC 3.4.13.22     
Accepted name: D-Ala-D-Ala dipeptidase
Reaction: D-Ala-D-Ala + H2O = 2 D-Ala
Other name(s): D-alanyl-D-alanine dipeptidase; vanX D-Ala-D-Ala dipeptidase; VanX
Comments: A Zn2+-dependent enzyme [4]. The enzyme protects Enterococcus faecium from the antibiotic vancomycin, which can bind to the -D-Ala-D-Ala sequence at the C-terminus of the peptidoglycan pentapeptide (see diagram). This enzyme reduces the availability of the free dipeptide D-Ala-D-Ala, which is the precursor for this pentapeptide sequence, allowing D-Ala-(R)-lactate (for which vancomycin has much less affinity) to be added to the cell wall instead [2,3]. The enzyme is stereospecific, as L-Ala-L-Ala, D-Ala-L-Ala and L-Ala-D-Ala are not substrates [2]. Belongs in peptidase family M15.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Reynolds, P.E., Depardieu, F., Dutka-Malen, S., Arthur, M. and Courvalin, P. Glycopeptide resistance mediated by enterococcal transposon Tn1546 requires production of VanX for hydrolysis of D-alanyl-D-alanine. Mol. Microbiol. 13 (1994) 1065–1070. [DOI] [PMID: 7854121]
2.  Wu, Z., Wright, G.D. and Walsh, C.T. Overexpression, purification, and characterization of VanX, a D-, D-dipeptidase which is essential for vancomycin resistance in Enterococcus faecium BM4147. Biochemistry 34 (1995) 2455–2463. [PMID: 7873524]
3.  McCafferty, D.G., Lessard, I.A. and Walsh, C.T. Mutational analysis of potential zinc-binding residues in the active site of the enterococcal D-Ala-D-Ala dipeptidase VanX. Biochemistry 36 (1997) 10498–10505. [DOI] [PMID: 9265630]
4.  Bussiere, D.E., Pratt, S.D., Katz, L., Severin, J.M., Holzman, T. and Park, C.H. The structure of VanX reveals a novel amino-dipeptidase involved in mediating transposon-based vancomycin resistance. Mol. Cell. 2 (1998) 75–84. [DOI] [PMID: 9702193]
5.  Tan, A.L., Loke, P. and Sim, T.S. Molecular cloning and functional characterisation of VanX, a D-alanyl-D-alanine dipeptidase from Streptomyces coelicolor A3(2). Res. Microbiol. 153 (2002) 27–32. [DOI] [PMID: 11881895]
6.  Matthews, M.L., Periyannan, G., Hajdin, C., Sidgel, T.K., Bennett, B. and Crowder, M.W. Probing the reaction mechanism of the D-ala-D-ala dipeptidase, VanX, by using stopped-flow kinetic and rapid-freeze quench EPR studies on the Co(II)-substituted enzyme. J. Am. Chem. Soc. 128 (2006) 13050–13051. [DOI] [PMID: 17017774]
[EC 3.4.13.22 created 2006]
 
 
EC 3.4.13.23     
Accepted name: cysteinylglycine-S-conjugate dipeptidase
Reaction: an [L-cysteinylglycine]-S-conjugate + H2O = an L-cysteine-S-conjugate + glycine
Other name(s): tpdA (gene name); LAP3 (gene name)
Systematic name: cysteinylglycine-S-conjugate dipeptide hydrolase
Comments: The enzyme participates in a widespread glutathione-mediated detoxification pathway. In animals the activity is usually catalysed by enzymes that have numerous additional activities, such as EC 3.4.11.1, leucyl aminopeptidase, EC 3.4.11.2, membrane alanyl aminopeptidase, and EC 3.4.13.19, membrane dipeptidase. However, in the bacterium Corynebacterium sp. Ax20, which degrades axillary secretions, the enzyme appears to be specific for this task.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  SEMENZA G Chromatographic purification of cysteinyl-glycinase. Biochim. Biophys. Acta 24 (1957) 401–413. [PMID: 13436444]
2.  Rankin, B.B., McIntyre, T.M. and Curthoys, N.P. Brush border membrane hydrolysis of S-benzyl-cysteine-p-nitroanilide, and activity of aminopeptidase M. Biochem. Biophys. Res. Commun. 96 (1980) 991–996. [PMID: 6108111]
3.  Hirota, T., Nishikawa, Y., Takahagi, H., Igarashi, T. and Kitagawa, H. Simultaneous purification and properties of dehydropeptidase-I and aminopeptidase-M from rat kidney. Res Commun Chem Pathol Pharmacol 49 (1985) 435–445. [PMID: 2865778]
4.  Josch, C., Klotz, L.O. and Sies, H. Identification of cytosolic leucyl aminopeptidase (EC 3.4.11.1) as the major cysteinylglycine-hydrolysing activity in rat liver. Biol. Chem. 384 (2003) 213–218. [PMID: 12675513]
5.  Emter, R. and Natsch, A. The sequential action of a dipeptidase and a β-lyase is required for the release of the human body odorant 3-methyl-3-sulfanylhexan-1-ol from a secreted Cys-Gly-(S) conjugate by Corynebacteria. J. Biol. Chem. 283 (2008) 20645–20652. [PMID: 18515361]
[EC 3.4.13.23 created 2019]
 
 
EC 3.4.14.1     
Accepted name: dipeptidyl-peptidase I
Reaction: Release of an N-terminal dipeptide, Xaa-Yaa┼Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro
Other name(s): cathepsin C; dipeptidyl aminopeptidase I; dipeptidyl transferase; dipeptide arylamidase I; DAP I
Comments: A Cl--dependent, lysosomal cysteine-type peptidase maximally active at acidic pH. Also polymerizes dipeptide amides, arylamides and esters at neutral pH. In peptidase family C1 (papain family).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9032-68-2
References:
1.  Planta, R.J., Gorter, J. and Gruber, M. The catalytic properties of cathepsin C. Biochim. Biophys. Acta 89 (1964) 511–519. [PMID: 14209333]
2.  Metrione, R.M., Neves, A.G. and Fruton, J.S. Purification and properties of dipeptidyl transferase (cathepsin C). Biochemistry 5 (1966) 1597–1604. [PMID: 5961281]
3.  McDonald, J.K., Zeitman, B.B., Reilly, T.J. and Ellis, S. New observations on the substrate specificity of cathepsin C (dipeptidyl aminopeptidase I) including the degradation of β-corticotropin and other peptide hormones. J. Biol. Chem. 244 (1969) 2693–2709. [PMID: 4306035]
4.  McDonald, J.K. and Schwabe, C. Intracellular exopeptidases. In: Barrett, A.J. (Ed.), Proteinases in Mammalian Cells and Tissues, North-Holland Publishing Co., Amsterdam, 1977, pp. 311–391.
[EC 3.4.14.1 created 1961 as EC 3.4.4.9, transferred 1972 to EC 3.4.14.1]
 
 
EC 3.4.14.2     
Accepted name: dipeptidyl-peptidase II
Reaction: Release of an N-terminal dipeptide, Xaa-Yaa┼, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides
Other name(s): dipeptidyl aminopeptidase II; dipeptidyl arylamidase II; carboxytripeptidase; dipeptidyl peptidase II; DAP II; dipeptidyl(amino)peptidase II; dipeptidylarylamidase
Comments: A lysosomal serine-type peptidase in family S28 (Pro-X carboxypeptidase family); maximally active at acidic pH
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 76199-23-0
References:
1.  McDonald, J.K., Reilly, T.J., Zeitman, B.B. and Ellis, S. Dipeptidyl arylamidase II of the pituitary. Properties of lysyl-alanyl-β-naphthylamide hydrolysis: inhibition by cations, distribution in tissues and subcellular localization. J. Biol. Chem. 243 (1968) 4143–4150. [PMID: 4969969]
2.  McDonald, J.K. and Schwabe, C. Intracellular exopeptidases. In: Barrett, A.J. (Ed.), Proteinases in Mammalian Cells and Tissues, North-Holland Publishing Co., Amsterdam, 1977, pp. 311–391.
[EC 3.4.14.2 created 1978]
 
 
EC 3.4.14.3      
Transferred entry: acylamino-acid-releasing enzyme. Now EC 3.4.19.1, acylaminoacyl-peptidase
[EC 3.4.14.3 created 1978, deleted 1981]
 
 
EC 3.4.14.4     
Accepted name: dipeptidyl-peptidase III
Reaction: Release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides.
Other name(s): dipeptidyl aminopeptidase III; dipeptidyl arylamidase III; enkephalinase B; red cell angiotensinase
Comments: A cytosolic peptidase that is active at neutral pH. It has broad activity on peptides, although it is highly selective for Arg-Arg-2-naphthylamide, at pH 9.2. Active in the hydrolysis of enkephalins. A metallopeptidase, the type example of peptidase family M49.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 77464-87-0
References:
1.  McDonald, J.K. Dipeptidyl-peptidase III. In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Ed.), Handbook of Proteolytic Enzymes, Handbook of Proteolytic Enzymes, London, 1998, pp. 536–538.
2.  Fukasawa, K., Fukasawa, K.M., Iwamoto, H., Hirose, J. and Harada, M. The HELLGH motif of rat liver dipeptidyl peptidase III is involved in zinc coordination and the catalytic activity of the enzyme. Biochemistry 38 (1999) 8299–8303. [DOI] [PMID: 10387075]
[EC 3.4.14.4 created 1981, modified 2001]
 
 
EC 3.4.14.5     
Accepted name: dipeptidyl-peptidase IV
Reaction: Release of an N-terminal dipeptide, Xaa-Yaa┼Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline
Other name(s): dipeptidyl aminopeptidase IV; Xaa-Pro-dipeptidyl-aminopeptidase; Gly-Pro naphthylamidase; postproline dipeptidyl aminopeptidase IV; lymphocyte antigen CD26; glycoprotein GP110; dipeptidyl peptidase IV; glycylproline aminopeptidase; X-prolyl dipeptidyl aminopeptidase; pep X; leukocyte antigen CD26; glycylprolyl dipeptidylaminopeptidase; dipeptidyl-peptide hydrolase; glycylprolyl aminopeptidase; dipeptidyl-aminopeptidase IV; DPP IV/CD26; amino acyl-prolyl dipeptidyl aminopeptidase; T cell triggering molecule Tp103; X-PDAP
Comments: A homodimer. An integral protein of the plasma membrane of lymphocytes and other mammalian cells, in peptidase family S9 (prolyl oligopeptidase family). The reaction is similar to that of the unrelated EC 3.4.14.11 Xaa-Pro dipeptidyl-peptidase of lactococci
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 54249-88-6
References:
1.  Misumi, Y., Hayashi, Y., Arakawa, F. and Ikehara, Y. Molecular cloning and sequence analysis of human dipeptidyl peptidase IV, a serine proteinase on the cell surface. Biochim. Biophys. Acta 1131 (1992) 333–336. [DOI] [PMID: 1352704]
2.  David, F., Bernard, A.-M., Pierres, M. and Marguet, D. Identification of serine 624, aspartic acid 702, and histidine 734 as the catalytic triad residues of mouse dipeptidyl-peptidase IV (CD26). A member of a novel family of nonclassical serine hydrolases. J. Biol. Chem. 268 (1993) 17247–17252. [PMID: 8102366]
3.  Ikehara, Y., Ogata, S. and Misumi, Y. Dipeptidyl-peptidase IV from rat liver. Methods Enzymol. 244 (1994) 215–227. [DOI] [PMID: 7845210]
[EC 3.4.14.5 created 1981, modified 1996]
 
 
EC 3.4.14.6     
Accepted name: dipeptidyl-dipeptidase
Reaction: Preferential release of dipeptides from a tetrapeptide, e.g. Ala-Gly┼Ala-Gly. Acts more slowly on Ala-Ala┼Ala-Ala and Gly-Gly┼Gly-Gly
Other name(s): dipeptidyl tetrapeptide hydrolase; dipeptidyl ligase; tetrapeptide dipeptidase
Comments: A thiol-activated peptidase from cabbage (Brassica oleracea). Tetrapeptides are formed from Ala-Ala, Gly-Gly, Ala-Gly and Gly-Ala
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 91608-92-3
References:
1.  Eng, F.W.H.T. Dipeptidyl tetrapeptide hydrolase, a new enzyme with dipeptidyl ligase activity. Can. J. Biochem. Cell. Biol. 62 (1984) 516–528.
[EC 3.4.14.6 created 1989]
 
 
EC 3.4.14.7      
Deleted entry:  tetralysine endopeptidase
[EC 3.4.14.7 created 1989, deleted 1992]
 
 
EC 3.4.14.8      
Transferred entry: tripeptidyl peptidase. Now EC 3.4.14.10, tripeptidyl-peptidase II
[EC 3.4.14.8 created 1989, deleted 1992]
 
 
EC 3.4.14.9     
Accepted name: tripeptidyl-peptidase I
Reaction: Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity.
Other name(s): tripeptidyl aminopeptidase; tripeptidyl peptidase
Comments: A lysosomal enzyme that is active at acidic pH. Deficient in classical late-infantile neuronal ceroid lipofuscinosis brain tissue. Belongs in peptidase family S53. Formerly included in EC 3.4.14.8.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 151662-36-1
References:
1.  Ezaki, J., Tanida, I., Kanehagi, N. and Kominami, E. A lysosomal proteinase, the late infantile neuronal ceroid lipofuscinosis gene (CLN2) product, is essential for degradation of a hydrophobic protein, the subunit c of ATP synthase. J. Neurochem. 72 (1999) 2573–2582. [DOI] [PMID: 10349869]
2.  Rawlings, N.D. and Barrett, A.J. Tripeptidyl-peptidase I is apparently the CLN2 protein absent in classical late-infantile neuronal ceroid lipofuscinosis. Biochim. Biophys. Acta 1429 (1999) 496–500. [DOI] [PMID: 9989235]
3.  Ezaki, J., Takeda-Ezaki, M., Oda, K. and Kominami, E. Characterization of endopeptidase activity of tripeptidyl peptidase-I/CLN2 protein which is deficient in classical late infantile neuronal ceroid lipofuscinosis. Biochem. Biophys. Res. Commun. 268 (2000) 904–908. [DOI] [PMID: 10679303]
4.  Junaid, M.A., Wu, G.X. and Pullarkat, R.K. Purification and characterization of bovine brain lysosomal pepstatin-insensitive proteinase, the gene product deficient in the human late-infantile neuronal ceroid lipofuscinosis. J. Neurochem. 74 (2000) 287–294. [DOI] [PMID: 10617131]
5.  Lin, L., Sohar, I., Lackland, H. and Lobel, P. The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH. J. Biol. Chem. 276 (2001) 2249–2255. [DOI] [PMID: 11054422]
[EC 3.4.14.9 created 1992 (part of EC 3.4.14.8 created 1989, incorporated 1992), modified 2000, modified 2001, modified 2003]
 
 
EC 3.4.14.10     
Accepted name: tripeptidyl-peptidase II
Reaction: Release of an N-terminal tripeptide from a polypeptide
Other name(s): tripeptidyl aminopeptidase; tripeptidyl peptidase; tripeptidyl aminopeptidase II; tripeptidyl peptidase II; TPP
Comments: A cytosolic enzyme in peptidase family S8 (subtilisin family). Active at neutral pH. Inhibited by diisopropyl fluorophosphate. Formerly included in EC 3.4.14.8
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 101149-94-4
References:
1.  Bålöw, R.M., Ragnarsson, U. and Zetterqvist, Ö. Tripeptidyl aminopeptidase in the extralysosomal fraction of rat liver. J. Biol. Chem. 258 (1983) 11622–11628. [PMID: 6352701]
2.  Bålöw, R.M., Tomkinson, B., Ragnarsson, U. and Zetterqvist, Ö. Purification, substrate specificity, and classification of tripeptidyl peptidase II. J. Biol. Chem. 261 (1986) 2409–2417. [PMID: 3511062]
3.  Tomkinson, B. and Zetterqvist, Ö. Immunological cross-reactivity between human tripeptidyl peptidase II and fibronectin. Biochem. J. 267 (1990) 149–154. [PMID: 1691635]
[EC 3.4.14.10 created 1992 (part of EC 3.4.14.8 created 1989, incorporated 1992)]
 
 
EC 3.4.14.11     
Accepted name: Xaa-Pro dipeptidyl-peptidase
Reaction: Hydrolyses Xaa-Pro┼ bonds to release unblocked, N-terminal dipeptides from substrates including Ala-Pro┼p-nitroanilide and (sequentially) Tyr-Pro┼Phe-Pro┼Gly-Pro┼Ile
Other name(s): X-prolyl dipeptidyl aminopeptidase; PepX; X-prolyl dipeptidyl peptidase; X-Pro dipeptidyl-peptidase
Comments: The intracellular enzyme from Lactococcus lactis (190-kDa) is the type example of peptidase family S15. The reaction is similar to that catalysed by dipeptidyl-peptidase IV of animals
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 54249-88-6
References:
1.  Zevaco, C., Monnet, V. and Gripon, J.-C. Intracellular X-prolyl dipeptidyl peptidase from Lactococcus lactis spp. lactis: purification and properties. J. Appl. Bacteriol. 68 (1990) 357–366.
2.  Meyer-Barton, E.C., Klein, J.R., Imam, M. and Plapp, R. Cloning and sequence analysis of the X-prolyl-dipeptidyl-aminopeptidase gene (pepX) from Lactobacillus delbrückii ssp. lactis DSM7290. Appl. Microbiol. Biotechnol. 40 (1993) 82–89. [PMID: 7765315]
3.  Habibi-Najafi, M.B. and Lee, B.H. Purification and characterization of X-prolyl dipeptidyl peptidase from Lactobacillus casei subsp. casei LLG. Appl. Microbiol. Biotechnol. 42 (1994) 280–286. [PMID: 7765768]
4.  Chich, J.-F., Gripon, J.-C. and Ribadeau-Dumas, B. Preparation of bacterial X-prolyl dipeptidyl aminopeptidase and its stabilization by organic cosolvents. Anal. Biochem. 224 (1995) 245–249. [DOI] [PMID: 7710078]
5.  Chich, J.-F., Chapot-Chartier, M.P., Ribadeau-Dumas, B. and Gripon, J.-C. Identification of the active site serine of the X-prolyl aminopeptidase from Lactococcus lactis. FEBS Lett. 314 (1995) 139–142.
[EC 3.4.14.11 created 1996]
 
 
EC 3.4.14.12     
Accepted name: Xaa-Xaa-Pro tripeptidyl-peptidase
Reaction: Hydrolysis of Xaa-Xaa-Pro┼Yaa- releasing the N-terminal tripeptide of a peptide with Pro as the third residue (position P1) and where Yaa is not proline
Other name(s): prolyltripeptidyl amino peptidase; prolyl tripeptidyl peptidase; prolyltripeptidyl aminopeptidase; PTP-A; TPP
Comments: This cell-surface-associated serine exopeptidase is found in the Gram-negative, anaerobic bacterium Porphyromonas gingivalis, which has been implicated in adult periodontal disease [1]. The enzyme releases the N-terminal tripeptide of peptides, such as interleukin-6. It has an absolute requirement for a proline residue at the P1 position but is completely inactivated by a proline residue at the P1′ position [1]. The size of the peptide does not affect the rate of reaction [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Banbula, A., Mak, P., Bugno, M., Silberring, J., Dubin, A., Nelson, D., Travis, J. and Potempa, J. Prolyl tripeptidyl peptidase from Porphyromonas gingivalis. A novel enzyme with possible pathological implications for the development of periodontitis. J. Biol. Chem. 274 (1999) 9246–9252. [DOI] [PMID: 10092598]
2.  Fujimura, S., Ueda, O., Shibata, Y. and Hirai, K. Isolation and properties of a tripeptidyl peptidase from a periodontal pathogen Prevotella nigrescens. FEMS Microbiol. Lett. 219 (2003) 305–309. [DOI] [PMID: 12620636]
[EC 3.4.14.12 created 2006]
 
 
EC 3.4.14.13     
Accepted name: γ-D-glutamyl-L-lysine dipeptidyl-peptidase
Reaction: The enzyme releases L-Ala-γ-D-Glu dipeptides from cell wall peptides via cleavage of an L-Ala-γ-D-Glu┼L-Lys bond.
Other name(s): YkfC
Comments: The enzyme, characterized from the bacterium Bacillus subtilis, is involved in the recycling of the murein peptide.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Schmidt, D.M., Hubbard, B.K. and Gerlt, J.A. Evolution of enzymatic activities in the enolase superfamily: functional assignment of unknown proteins in Bacillus subtilis and Escherichia coli as L-Ala-D/L-Glu epimerases. Biochemistry 40 (2001) 15707–15715. [DOI] [PMID: 11747447]
2.  Xu, Q., Abdubek, P., Astakhova, T., Axelrod, H.L., Bakolitsa, C., Cai, X., Carlton, D., Chen, C., Chiu, H.J., Chiu, M., Clayton, T., Das, D., Deller, M.C., Duan, L., Ellrott, K., Farr, C.L., Feuerhelm, J., Grant, J.C., Grzechnik, A., Han, G.W., Jaroszewski, L., Jin, K.K., Klock, H.E., Knuth, M.W., Kozbial, P., Krishna, S.S., Kumar, A., Lam, W.W., Marciano, D., Miller, M.D., Morse, A.T., Nigoghossian, E., Nopakun, A., Okach, L., Puckett, C., Reyes, R., Tien, H.J., Trame, C.B., van den Bedem, H., Weekes, D., Wooten, T., Yeh, A., Hodgson, K.O., Wooley, J., Elsliger, M.A., Deacon, A.M., Godzik, A., Lesley, S.A. and Wilson, I.A. Structure of the γ-D-glutamyl-L-diamino acid endopeptidase YkfC from Bacillus cereus in complex with L-Ala-γ-D-Glu: insights into substrate recognition by NlpC/P60 cysteine peptidases. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66 (2010) 1354–1364. [DOI] [PMID: 20944232]
[EC 3.4.14.13 created 2015]
 
 
EC 3.4.14.14     
Accepted name: [mycofactocin precursor peptide] peptidase
Reaction: C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one + H2O = C-terminal [mycofactocin precursor peptide]-glycine + 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one
Glossary: 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one = AHDP
Other name(s): mftE (gene name)
Systematic name: C-terminal [mycofactocin precursor peptide]-glycyl-3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one hydrolyase
Comments: Requires Fe2+ ad Zn2+. The enzyme participates in the biosynthesis of the enzyme cofactor mycofactocin. It catalyses cleavage of the mycofactocin precursor peptide following its modification by MftC to liberate its final two residues, which consist of a cross-linked valine-tyramine dipeptide.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bruender, N.A. and Bandarian, V. The creatininase homolog MftE from Mycobacterium smegmatis catalyzes a peptide cleavage reaction in the biosynthesis of a novel ribosomally synthesized post-translationally modified peptide (RiPP). J. Biol. Chem. 292 (2017) 4371–4381. [DOI] [PMID: 28077628]
2.  Ayikpoe, R., Salazar, J., Majestic, B. and Latham, J.A. Mycofactocin biosynthesis proceeds through 3-amino-5-[(p-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidinone (AHDP); direct observation of MftE specificity toward MftA. Biochemistry 57 (2018) 5379–5383. [DOI] [PMID: 30183269]
[EC 3.4.14.14 created 2021]
 
 
EC 3.4.15.1     
Accepted name: peptidyl-dipeptidase A
Reaction: Release of a C-terminal dipeptide, oligopeptide┼Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II
Glossary: captopril = (2S)-1-(2-methyl-3-sulfanylpropanoyl)-L-proline
Other name(s): dipeptidyl carboxypeptidase I; peptidase P; dipeptide hydrolase (ambiguous); peptidyl dipeptidase; angiotensin converting enzyme; kininase II; angiotensin I-converting enzyme; carboxycathepsin; dipeptidyl carboxypeptidase; peptidyl dipeptidase I; peptidyl-dipeptide hydrolase; peptidyldipeptide hydrolase; endothelial cell peptidyl dipeptidase; ACE; peptidyl dipeptidase-4; PDH; peptidyl dipeptide hydrolase; DCP
Comments: A Cl--dependent, zinc glycoprotein that is generally membrane-bound. A potent inhibitor is captopril. Important in elevation of blood pressure, through formation of angiotensin II (vasoconstrictor) and destruction of bradykinin (vasodilator). Two molecular forms exist in mammalian tissues, a widely-distributed somatic form of 150- to 180-kDa that contains two non-identical catalytic sites, and a testicular form of 90- to 100-kDa that contains only a single catalytic site. Type example of peptidase family M2
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9015-82-1
References:
1.  Soubrier, F., Alhenc-Gelas, F., Hubert, C., Allegrini, J., John, M., Tregear, G. and Corvol, P. Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning. Proc. Natl. Acad. Sci. USA 85 (1988) 9386–9390. [DOI] [PMID: 2849100]
2.  Ehlers, M.R.W., Fox, E.A., Strydom, D.J. and Riordan, J.F. Molecular cloning of human testicular angiotensin-converting enzyme: the testis enzyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme. Proc. Natl. Acad. Sci. USA 86 (1989) 7741–7745. [DOI] [PMID: 2554286]
3.  Wei, L., Clauser, E., Alhenc-Gelas, F. and Corvol, P. The two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors. J. Biol. Chem. 267 (1992) 13398–13405. [PMID: 1320019]
4.  Corvol, P., Williams, T.A. and Soubrier, F. Peptidyl dipeptidase A: angiotensin I-converting enzyme. Methods Enzymol. 248 (1995) 283–305. [PMID: 7674927]
[EC 3.4.15.1 created 1972, modified 1981, modified 1989, modified 1996, modified 2011]
 
 
EC 3.4.15.2      
Transferred entry: pepdidyl carboxyamidase. Now EC 3.4.19.2, peptidyl-glycinamidase
[EC 3.4.15.2 created 1978, deleted 1981]
 
 
EC 3.4.15.3      
Transferred entry: dipeptidyl carboxypeptidase. Now EC 3.4.15.5, peptidyl-dipeptidase Dcp
[EC 3.4.15.3 created 1981, modified 1989, deleted 1996]
 
 
EC 3.4.15.4     
Accepted name: peptidyl-dipeptidase B
Reaction: Release of a C-terminal dipeptide or exceptionally a tripeptide
Other name(s): dipeptidyl carboxyhydrolase; atriopeptin convertase; atrial di-(tri)peptidyl carboxyhydrolase; peptidyldipeptidase B; atrial dipeptidyl carboxyhydrolase; atrial peptide convertase
Comments: A membrane-bound, zinc metallopeptidase located in mammalian atrial, but not ventricular, myocytes. Although it is capable of converting the 126-residue atriopeptin III directly to atriopeptin I by releasing a C-terminal tripeptide Phe-Arg-Tyr, it is generally restricted to the release of dipeptides. In contrast to peptidyl-dipeptidase A (EC 3.4.15.1) it displays no Cl- dependence and shows no action on angiotensin I. Conversely, peptidyl-dipeptidase A is unable to release Phe-Arg from the C-terminus of atriopeptin II
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 147014-93-5
References:
1.  Harris, R.B. and Wilson, I.B. Atrial tissue contains a metallo dipeptidyl carboxyhydrolase not present in ventricular tissue: partial purification and characterization. Arch. Biochem. Biophys. 233 (1984) 667–675. [DOI] [PMID: 6385859]
2.  Harris, R.B. and Wilson, I.B. Conversion of atriopeptin II to atriopeptin I by atrial dipeptidyl carboxy hydrolase. Peptides (Fayetteville) 6 (1985) 393–396. [DOI] [PMID: 2999723]
3.  Soler, D.F. and Harris, R.B. Continuous fluorogenic substrates for atrial dipeptidyl carboxyhydrolase. Importance of Ser in the P1 position. Int. J. Peptide Protein Res. 32 (1988) 35–40. [DOI] [PMID: 3146555]
4.  Soler, D.F. and Harris, R.B. Atrial dipeptidyl carboxyhydrolase is a zinc-metallo proteinase which possesses tripeptidyl carboxyhydrolase activity. Peptides (Fayetteville) 10 (1989) 63–68. [DOI] [PMID: 2501770]
[EC 3.4.15.4 created 1992]
 
 
EC 3.4.15.5     
Accepted name: peptidyl-dipeptidase Dcp
Reaction: Hydrolysis of unblocked, C-terminal dipeptides from oligopeptides, with broad specificity. Does not hydrolyse bonds in which P1′ is Pro, or both P1 and P1′ are Gly
Other name(s): dipeptidyl carboxypeptidase (Dcp); dipeptidyl carboxypeptidase
Comments: Known from Escherichia coli and Salmonella typhimurium. A zinc metallopeptidase in peptidase family M3 (thimet oligopeptidase family). Ac-Ala┼Ala-Ala is a good test substrate [3]. Inhibited by captopril, as is peptidyl-dipeptidase A. Formerly EC 3.4.15.3, and included in EC 3.4.15.1, peptidyl-dipeptidase A.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 395642-28-1
References:
1.  Yaron, A. Dipeptidyl carboxypeptidase from Escherichia coli. Methods Enzymol. 45 (1976) 599–610. [DOI] [PMID: 13271]
2.  Henrich, B., Becker, S., Schroeder, U. and Plapp, R. dcp gene of Escherichia coli: cloning, sequencing, transcript mapping, and characterization of the gene product. J. Bacteriol. 175 (1993) 7290–7300. [DOI] [PMID: 8226676]
3.  Conlin, C.A. and Miller, C.G. Oligopeptidase A and peptidyl-dipeptidase of Escherichia and Salmonella. Methods Enzymol. 248 (1995) 567–579. [PMID: 7674945]
[EC 3.4.15.5 created 1981 as EC 3.4.15.3, modified 1989, transferred 1996 to EC 3.4.15.5]
 
 
EC 3.4.15.6     
Accepted name: cyanophycinase
Reaction: [L-Asp(4-L-Arg)]n + H2O = [L-Asp(4-L-Arg)]n-1 + L-Asp(4-L-Arg)
For diagram of cyanophycin biosynthesis, click here
Glossary: cyanophycin = [L-Asp(4-L-Arg)]n = N-β-aspartylarginine = [L-4-(L-arginin-2-N-yl)aspartic acid]n = poly{N4-[(1S)-1-carboxy-4-guanidinobutyl]-L-asparagine}
Other name(s): cyanophycin degrading enzyme; β-Asp-Arg hydrolysing enzyme; CGPase; CphB; CphE; cyanophycin granule polypeptidase; extracellular CGPase
Comments: The enzyme is highly specific for the branched polypeptide cyanophycin and does not hydrolyse poly-L-aspartate or poly-L-arginine [3]. A serine-type exopeptidase that belongs in peptidase family S51.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 131554-16-0
References:
1.  Obst, M., Krug, A., Luftmann, H. and Steinbüchel, A. Degradation of cyanophycin by Sedimentibacter hongkongensis strain KI and Citrobacter amalonaticus strain G isolated from an anaerobic bacterial consortium. Appl. Environ. Microbiol. 71 (2005) 3642–3652. [DOI] [PMID: 16000772]
2.  Obst, M., Oppermann-Sanio, F.B., Luftmann, H. and Steinbüchel, A. Isolation of cyanophycin-degrading bacteria, cloning and characterization of an extracellular cyanophycinase gene (cphE) from Pseudomonas anguilliseptica strain BI. The cphE gene from P. anguilliseptica BI encodes a cyanophycin-hydrolyzing enzyme. J. Biol. Chem. 277 (2002) 25096–25105. [DOI] [PMID: 11986309]
3.  Richter, R., Hejazi, M., Kraft, R., Ziegler, K. and Lockau, W. Cyanophycinase, a peptidase degrading the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartic acid (cyanophycin): molecular cloning of the gene of Synechocystis sp. PCC 6803, expression in Escherichia coli, and biochemical characterization of the purified enzyme. Eur. J. Biochem. 263 (1999) 163–169. [DOI] [PMID: 10429200]
[EC 3.4.15.6 created 2007]
 
 
EC 3.4.16.1      
Transferred entry: serine carboxypeptidase. Now EC 3.4.16.6, carboxypeptidase D
[EC 3.4.16.1 created 1972 as EC 3.4.12.1 and EC 3.4.21.13, both transferred 1978 to EC 3.4.16.1, deleted 1993]
 
 
EC 3.4.16.2     
Accepted name: lysosomal Pro-Xaa carboxypeptidase
Reaction: Cleavage of a -Pro┼Xaa bond to release a C-terminal amino acid
Other name(s): angiotensinase C; lysosomal carboxypeptidase C; peptidylprolylamino acid carboxypeptidase; aminoacylproline carboxypeptidase; prolyl carboxypeptidase; carboxypeptidase P; proline-specific carboxypeptidase P; PCP
Comments: A lysosomal peptidase active at acidic pH that inactivates angiotensin II. Inhibited by diisopropyl fluorophosphate. In peptidase family S28 (Pro-X carboxypeptidase family).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9075-64-3
References:
1.  Walter, R., Simmons, W.H. and Yoshimoto, T. Proline specific endo- and exopeptidases. Mol. Cell. Biochem. 30 (1980) 111–127. [PMID: 6991912]
2.  Odya, C.E. and Erdös, E.G. Human prolylcarboxypeptidase. Methods Enzymol. 80 (1981) 460–466. [PMID: 7341916]
[EC 3.4.16.2 created 1972 as EC 3.4.12.4, transferred 1978 to EC 3.4.16.2]
 
 
EC 3.4.16.3      
Transferred entry: tyrosine carboxypeptidase. Now included with EC 3.4.16.5, carboxypeptidase C
[EC 3.4.16.3 created 1972 as EC 3.4.12.12, transferred 1978 to EC 3.4.16.3, deleted 1992]
 
 
EC 3.4.16.4     
Accepted name: serine-type D-Ala-D-Ala carboxypeptidase
Reaction: Preferential cleavage: (Ac)2-L-Lys-D-Ala┼D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine
Other name(s): DD-peptidase; D-alanyl-D-alanine-carboxypeptidase; D-alanyl-D-alanine-cleaving-peptidase; D-alanyl-D-alanine-cleaving peptidase; DD-transpeptidase; D-alanine carboxypeptidase; DD-carboxypeptidase; D-alanyl carboxypeptidase
Comments: A membrane-bound, bacterial enzyme inhibited by penicillin and other β-lactam antibiotics, which acylate the active site serine. Examples are known from peptidase families S11, S12 and S13. Distinct from EC 3.4.17.14, zinc D-Ala-D-Ala carboxypeptidase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9077-67-2
References:
1.  Ghuysen, J.-M., Frère, J.-M., Leyh-Bouille, M., Nguyen-Distèche, M., Coyette, J., Dusart, J., Joris, B., Duez, C., Dideberg, O., Charlier, P., Dive, G. and Lamotte-Brasseur, J. Bacterial wall peptidoglycan, DD-peptidases and β-lactam antibiotics. Scand. J. Infect. Dis. Suppl. 42 (1984) 17–37. [PMID: 6597561]
2.  Frère, J.M. and Joris, B. Penicillin-sensitive enzymes in peptidoglycan biosynthesis. CRC Crit. Rev. Microbiol. 11 (1985) 306–331. [PMID: 3888533]
[EC 3.4.16.4 created 1989]
 
 
EC 3.4.16.5     
Accepted name: carboxypeptidase C
Reaction: Release of a C-terminal amino acid with broad specificity
Other name(s): carboxypeptidase Y; serine carboxypeptidase I; cathepsin A; lysosomal protective protein; deamidase; lysosomal carboxypeptidase A; phaseolin
Comments: A carboxypeptidase with optimum pH 4.5–6.0, inhibited by diisopropyl fluorophosphate, and sensitive to thiol-blocking reagents (reviewed in [1]). Widely distributed in eukaryotes. Type example of peptidase family S10.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9046-67-7
References:
1.  Breddam, K. Serine carboxypeptidases. A review. Carlsberg Res. Commun. 51 (1986) 83–128.
2.  Valls, L.A., Hunter, C.P., Rothman, J.H. and Stevens, T.H. Protein sorting in yeast: the localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide. Cell 48 (1987) 887–897. [DOI] [PMID: 3028649]
3.  Jackman, H.L., Morris, P.W., Deddish, P.A., Skidgel, R.A. and Erdös, E.G. Inactivation of endothelin I by deamidase (lysosomal protective protein). J. Biol. Chem. 267 (1992) 2872–2875. [PMID: 1737744]
4.  Miller, J.J., Changaris, D.G. and Levy, R.S. Purification, subunit structure and inhibitor profile of cathepsin-A. J. Chromatogr. 627 (1992) 153–162. [PMID: 1487525]
[EC 3.4.16.5 created 1972 as EC 3.4.12.1, transferred 1978 to EC 3.4.16.1, part transferred 1993 to EC 3.4.16.5 (EC 3.4.16.3 created 1972 as EC 3.4.12.12, transferred 1978 to EC 3.4.16.3, transferred 1992 to EC 3.4.16.1), (EC 3.4.21.13 created 1972, transferred 1978 to EC 3.4.16.1)]
 
 
EC 3.4.16.6     
Accepted name: carboxypeptidase D
Reaction: Preferential release of a C-terminal arginine or lysine residue
Other name(s): cereal serine carboxypeptidase II; Saccharomyces cerevisiae KEX1 gene product; carboxypeptidase Kex1; gene KEX1 serine carboxypeptidase; KEX1 carboxypeptidase; KEX1 proteinase; KEX1DELTAp; CPDW-II; serine carboxypeptidase (misleading); Phaseolus proteinase
Comments: A carboxypeptidase with optimum pH 4.5-6.0, inhibited by diisopropyl fluorophosphate, and sensitive to thiol-blocking reagents (reviewed in [1]). In peptidase family S10 (carboxypeptidase C family).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 153967-26-1
References:
1.  Breddam, K. Serine carboxypeptidases. A review. Carlsberg Res. Commun. 51 (1986) 83–128.
2.  Breddam, K., Sørensen, S.B. and Svendsen, I. Primary structure and enzymatic properties of carboxypeptidase II from wheat bran. Carlsberg Res. Commun. 52 (1987) 297–311.
3.  Dmochowska, A., Dignard, D., Henning, D., Thomas, D.Y. and Bussey, H. Yeast KEX1 gene encodes a putative protease with a carboxypeptidase B-like function involved in killer toxin and α-factor precursor processing. Cell 50 (1987) 573–584. [DOI] [PMID: 3301004]
4.  Liao, D.-I., Breddam, K., Sweet, R.M., Bullock, T. and Remington, S.J. Refined atomic model of wheat serine carboxypeptidase II at 2.2-Å resolution. Biochemistry 31 (1992) 9796–9812. [PMID: 1390755]
[EC 3.4.16.6 created 1972 as EC 3.4.12.1, transferred 1978 to EC 3.4.16.1, part transferred 1993 to EC 3.4.16.6 (EC 3.4.16.3 created 1972 as EC 3.4.12.12, transferred 1978 to EC 3.4.16.3, transferred 1992 to EC 3.4.16.1), (EC 3.4.21.13 created 1972, transferred 1978 to EC 3.4.16.1), modified 2011]
 
 
EC 3.4.17.1     
Accepted name: carboxypeptidase A
Reaction: Release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro
Other name(s): carboxypolypeptidase; pancreatic carboxypeptidase A; tissue carboxypeptidase A
Comments: A zinc enzyme formed from procarboxypeptidase A. Isolated from cattle, pig and dogfish pancreas, and other sources including mast cells [3] and skeletal muscle [4]. Type example of peptidase family M14.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 11075-17-5
References:
1.  Petra, P.H. Bovine procarboxypeptidase and carboxypeptidase A. Methods Enzymol. 19 (1970) 460–503.
2.  Reeck, G.R., Walsh, K.A. and Neurath, H. Isolation and characterization of carboxypeptidases A and B from activated pancreatic juice. Biochemistry 10 (1971) 4690–4698. [PMID: 5140186]
3.  Everitt, M.T. and Neurath, H. Rat peritoneal mast cell carboxypeptidase: localization, purification and enzymatic properties. FEBS Lett. 110 (1980) 292–296. [DOI] [PMID: 7371832]
4.  Bodwell, J.E. and Meyer, W.L. Purification and characterization of carboxypeptidase A from rat skeletal muscle. Biochemistry 20 (1981) 2767–2777. [PMID: 7018567]
[EC 3.4.17.1 created 1961 as EC 3.4.2.1, transferred 1972 to EC 3.4.12.2, transferred 1978 to EC 3.4.17.1]
 
 
EC 3.4.17.2     
Accepted name: carboxypeptidase B
Reaction: Preferential release of a C-terminal lysine or arginine amino acid
Other name(s): protaminase; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase
Comments: A zinc enzyme formed from procarboxypeptidase B. Isolated from cattle, pig and dogfish pancreas and other sources, including skin fibroblasts [3] and adrenal medulla [4]. In peptidase family M14 (carboxypeptidase A family).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9025-24-5
References:
1.  Folk, J.E. Carboxypeptidase B (porcine pancreas). Methods Enzymol. 19 (1970) 504–508.
2.  Brodrick, J.W., Geokas, M.C. and Largman, C. Human carboxypeptidase B. II. Purification of the enzyme from pancreatic tissue and comparison with the enzymes present in pancreatic secretion. Biochim. Biophys. Acta 452 (1976) 468–481. [DOI] [PMID: 1009123]
3.  Butterworth, J. and Duncan, J.J. Carboxypeptidase B activity of cultured skin fibroblasts and relationship to cystic fibrosis. Clin. Chim. Acta 97 (1979) 39–43. [DOI] [PMID: 40714]
4.  Wallace, E.F., Evans, C.J., Jurik, S.M., Mefford, I.N. and Barchas, J.D. Carboxypeptidase B activity from adrenal medulla. Is it involved in the processing of proenkephalin? Life Sci. 31 (1982) 1793–1796. [PMID: 6130442]
[EC 3.4.17.2 created 1961 as EC 3.4.2.2, transferred 1972 to EC 3.4.12.3, transferred 1978 to EC 3.4.17.2]
 
 
EC 3.4.17.3     
Accepted name: lysine carboxypeptidase
Reaction: Release of a C-terminal basic amino acid, preferentially lysine
Other name(s): carboxypeptidase N; arginine carboxypeptidase; kininase I; anaphylatoxin inactivator; plasma carboxypeptidase B; creatine kinase conversion factor; bradykinase; kininase Ia; hippuryllysine hydrolase; bradykinin-decomposing enzyme; protaminase; CPase N; creatinine kinase convertase; peptidyl-L-lysine(-L-arginine) hydrolase; CPN
Comments: A zinc enzyme found in plasma. Inactivates bradykinin and anaphylatoxins in blood plasma. In peptidase family M14 (carboxypeptidase A family).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9013-89-2
References:
1.  Plummer, T.H., Jr. and Erdös, E.G. Human plasma carboxypeptidase N. Methods Enzymol. 80 (1981) 442–449. [PMID: 7341915]
2.  Levin, Y., Skidgel, R.A. and Erdös, E.G. Isolation and characterization of the subunits of human plasma carboxypeptidase N (kininase I). Proc. Natl. Acad. Sci. USA 79 (1982) 4618–4622. [DOI] [PMID: 6750606]
3.  Skidgel, R.A. Basic carboxypeptidases: regulators of peptide hormone activity. Trends Pharmacol. Sci. 9 (1988) 301–303. [DOI] [PMID: 3074547]
[EC 3.4.17.3 created 1972 as EC 3.4.12.7, transferred 1978 to EC 3.4.17.3, modified 1989]
 
 
EC 3.4.17.4     
Accepted name: Gly-Xaa carboxypeptidase
Reaction: Release of a C-terminal amino acid from a peptide in which glycine is the penultimate amino acid, e.g. Z-Gly┼Leu
Other name(s): glycine carboxypeptidase; carboxypeptidase a; carboxypeptidase S; peptidase α; yeast carboxypeptidase; Gly-X carboxypeptidase
Comments: From yeast. In peptidase family M20 (glutamate carboxypeptidase family).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9025-25-6
References:
1.  Félix, F. and Brouillet, N. Purification et proprietes de deux peptidases de levure de brasserie. Biochim. Biophys. Acta 122 (1966) 127–144. [PMID: 4961236]
2.  Wolf, D.H. and Ehmann, C. Carboxypeptidase S from yeast: regulation of its activity during vegetative growth and differentiation. FEBS Lett. 91 (1978) 59–62. [DOI] [PMID: 352726]
[EC 3.4.17.4 created 1961 as EC 3.4.2.3, transferred 1972 to EC 3.4.12.8, transferred 1978 to EC 3.4.17.4 (EC 3.4.17.9 created 1981, incorporated 1992)]
 
 
EC 3.4.17.5      
Deleted entry: aspartate carboxypeptidase
[EC 3.4.17.5 created 1972 as EC 3.4.12.9, transferred 1978 to EC 3.4.17.5, deleted 1992]
 
 
EC 3.4.17.6     
Accepted name: alanine carboxypeptidase
Reaction: Release of a C-terminal alanine from a peptide or a variety of pteroyl or acyl groups
Other name(s): N-benzoyl-L-alanine-amidohydrolase
Comments: From soil bacteria. The enzyme from Corynebacterium equi also hydrolyses N-benzoylglycine and N-benzoyl-L-aminobutyric acid.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 37288-70-3
References:
1.  Levy, C.C. and Goldman, P. Bacterial peptidases. J. Biol. Chem. 244 (1969) 4467–4472. [PMID: 5806587]
2.  Miyagawa, E., Takahiro, H. and Yoshinobu, M. Purification and properties of N-benzoyl-L-alanine amidohydrolase from Corynebacterium equii. Agric. Biol. Chem. 50 (1986) 1527–1531.
[EC 3.4.17.6 created 1972 as EC 3.4.12.11, transferred 1978 to EC 3.4.17.6]
 
 
EC 3.4.17.7      
Transferred entry: acylmuramoyl-alanine carboxypeptidase. Now EC 3.5.1.28, N-acetylmuramoyl-L-alanine amidase
[EC 3.4.17.7 created 1978, deleted 1992]
 
 
EC 3.4.17.8     
Accepted name: muramoylpentapeptide carboxypeptidase
Reaction: Cleavage of the bond UDP-N-acetylmuramoyl-L-alanyl-γ-D-glutamyl-6-carboxy-L-lysyl-D-alanyl┼D-alanine
Other name(s): D-alanine carboxypeptidase I; DD-carboxypeptidase; D-alanine carboxypeptidase; D-alanyl-D-alanine carboxypeptidase; D-alanine-D-alanine-carboxypeptidase; carboxypeptidase D-alanyl-D-alanine; carboxypeptidase I; UDP-N-acetylmuramoyl-tetrapeptidyl-D-alanine alanine-hydrolase; D-alanyl-D-alanine peptidase; DD-peptidase; penicillin binding protein 5; PBP5; PdcA; VanY
Comments: A bacterial enzyme that requires a divalent cation for activity. Does not cleave the C-terminal D-alanine from the product of the above reaction, UDP-N-acetyl-muramoyl-L-alanyl-γ-D-glutamyl-6-carboxy-L-lysyl-D-alanine. Competitively inhibited by penicillins and cephalosporins.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9077-67-2
References:
1.  Izaki, K. and Strominger, J.L. Biosynthesis of the peptidoglycan of bacterial cell walls. XIV. Purification and properties of two D-alanine carboxypeptidases from Escherichia coli. J. Biol. Chem. 243 (1968) 3193–3201. [PMID: 4871206]
[EC 3.4.17.8 created 1972 as EC 3.4.12.6, transferred 1978 to EC 3.4.17.8]
 
 
EC 3.4.17.9      
Transferred entry: carboxypeptidase S. Now included with EC 3.4.17.4, Gly-Xaa carboxypeptidase
[EC 3.4.17.9 created 1981, deleted 1992]
 
 
EC 3.4.17.10     
Accepted name: carboxypeptidase E
Reaction: Release of C-terminal arginine or lysine residues from polypeptides
Other name(s): carboxypeptidase H; enkephalin convertase; cobalt-stimulated chromaffin granule carboxypeptidase; insulin granule-associated carboxypeptidase; enkephalin convertase; membrane-bound carboxypeptidase; carboxypeptidase E; enkephalin-precursor endopeptidase; enkephalin precursor carboxypeptidase; peptidyl-L-lysine(-L-arginine) hydrolase
Comments: A zinc enzyme, activated by Co2+. Inhibited by 1,10-phenanthroline and other chelating agents. pH optimum 5.6. Located in storage granules of secretory cells, and active in processing of protein hormones and bioactive peptides. In peptidase family M14 (carboxypeptidase A family).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81876-95-1
References:
1.  Qian, Y.M., Varlamov, O. and Fricker, L.D. Glu300 of rat carboxypeptidase E is essential for enzymatic activity but not substrate binding or routing to the regulated secretory pathway. J. Biol. Chem. 274 (1999) 11582–11586. [DOI] [PMID: 10206965]
2.  Fricker, L.D. Carboxypeptidase E/H. In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Ed.), Handbook of Proteolytic Enzymes, Academic Press, London, 1998, pp. 1341–1344.
3.  Fricker, L.D. Methods for studying carboxypeptidase E. Methods Neurosci. 23 (1995) 237–250.
4.  Manser, E., Fernandez, D. , Loo,L., Goh, P.Y., Monfries, C., Hall, C. and Lim, L. Human carboxypeptidase E: isolation and characterisaton of the cDNA, sequence conservation, expression and processing in vitro. Biochem. J. 267 (1990) 517–525. [PMID: 2334405]
5.  Fricker, L.D. Carboxypeptidase E. Annu. Rev. Physiol. 50 (1988) 309–321. [DOI] [PMID: 2897826]
[EC 3.4.17.10 created 1986, modified 2000]
 
 
EC 3.4.17.11     
Accepted name: glutamate carboxypeptidase
Reaction: Release of C-terminal glutamate residues from a wide range of N-acylating moieties, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl and pteroyl groups
Other name(s): carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; glutamyl carboxypeptidase; N-pteroyl-L-glutamate hydrolase
Comments: A zinc enzyme produced by pseudomonads, Flavobacterium sp. and Acinetobacter sp. Its ability to hydrolyse pteroyl-L-glutamate (folic acid) has led to its use as a folate-depleting, antitumour agent. Type example of peptidase family M20
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9074-87-7
References:
1.  Goldman, P. and Levy, C.C. Carboxypeptidase G: purification and properties. Proc. Natl. Acad. Sci. USA 58 (1967) 1299–1306. [DOI] [PMID: 5237864]
2.  McCullogh, J.L., Chabner, B.A. and Bertino, J.R. Purification and properties of carboxypeptidase G1. J. Biol. Chem. 246 (1971) 7207–7213. [PMID: 5129727]
3.  Albrecht, A.M., Boldizar, E. and Hutchinson, D.J. Carboxypeptidase displaying differential velocity in hydrolysis of methotrexate, 5-methyltetrahydrofolic acid, and leucovorin. J. Bacteriol. 134 (1978) 506–513. [PMID: 26657]
4.  Sherwood, R.F., Melton, R.G. and Alwan, S.A. Purification and properties of carboxypeptidase G2 from Pseudomonas sp. strain RS-16. Eur. J. Biochem. 148 (1985) 447–453. [DOI] [PMID: 3838935]
[EC 3.4.17.11 created 1992]
 
 
EC 3.4.17.12     
Accepted name: carboxypeptidase M
Reaction: Cleavage of C-terminal arginine or lysine residues from polypeptides
Other name(s): CPM
Comments: A membrane-bound enzyme optimally active at neutral pH. In peptidase family M14 (carboxypeptidase A family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 120038-28-0
References:
1.  Skidgel, R.A. Basic carboxypeptidases: Regulators of peptide hormone activity. Trends Pharmacol. Sci. 9 (1988) 303–304. [DOI] [PMID: 3074547]
2.  Deddish, P.A., Skidgel, R.A. and Erdös, E.G. Enhanced Co2+ activation and inhibitor binding of carboxypeptidase M at low pH. Biochem. J. 261 (1989) 289–291. [PMID: 2775217]
3.  Skidgel, R.A., Davis, R.M. and Tan, F. Human carboxypeptidase M. Purification and characterization of membrane-bound carboxypeptidase that cleaves peptide hormones. J. Biol. Chem. 264 (1989) 2236–2241. [PMID: 2914904]
[EC 3.4.17.12 created 1992]
 
 
EC 3.4.17.13     
Accepted name: muramoyltetrapeptide carboxypeptidase
Reaction: Hydrolysis of the bond: N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-Ala-D-glutamyl-6-carboxy-L-lysyl┼D-alanine
Other name(s): carboxypeptidase IIW; carboxypeptidase II; lysyl-D-alanine carboxypeptidase; L-lysyl-D-alanine carboxypeptidase; LD-carboxypeptidase
Comments: Variants are known from various microorganisms. Involved in peptidoglycan synthesis, catalysing both decarboxylation and transpeptidation. Stimulated by divalent cations such as Mg2+ and Ca2+, but not by Zn2+. Inhibited by thiol-blocking reagents, but unaffected by penicillin
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 60063-80-1
References:
1.  DasGupta, H. and Fan, D.P. Purification and characterization of a carboxypeptidase-transpeptidase of Bacillus megaterium acting on the tetrapeptide moiety of the peptidoglycan. J. Biol. Chem. 254 (1979) 5672–5683. [PMID: 109439]
2.  Rousset, A., Nguyen-Disteche, M., Minck, R. and Ghuysen, J.-M. Penicillin-binding proteins and carboxypeptidase/transpeptidase activities in Proteus vulgaris P18 and its penicillin-induced stable L-forms. J. Bacteriol. 152 (1982) 1042–1048. [PMID: 6754695]
3.  Metz, R., Henning, S. and Hammes, W.P. LD-Carboxypeptidase activity in Escherichia coli. II. Isolation, purification and characterization of the enzyme from E. coli K 12. Arch. Microbiol. 144 (1986) 181–186. [PMID: 3521530]
[EC 3.4.17.13 created 1992]
 
 
EC 3.4.17.14     
Accepted name: zinc D-Ala-D-Ala carboxypeptidase
Reaction: Cleavage of the bond: (Ac)2-L-lysyl-D-alanyl┼D-alanine
Other name(s): Zn2+ G peptidase; D-alanyl-D-alanine hydrolase; D-alanyl-D-alanine-cleaving carboxypeptidase; DD-carboxypeptidase; G enzyme; DD-carboxypeptidase-transpeptidase
Comments: A zinc enzyme. Catalyses carboxypeptidation but not transpeptidation reactions involved in bacterial cell wall metabolism. Weakly inhibited by β-lactams. In peptidase family M15. Distinct from EC 3.4.16.4, serine-type D-Ala-D-Ala carboxypeptidase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 213189-85-6
References:
1.  Dideberg, O., Charlier, P., Dive, G., Joris, B., Frère, J.M. and Ghuysen, J.M. Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 Å resolution. Nature 299 (1982) 469–470. [PMID: 7121588]
2.  Joris, B., Van Beeumen, J., Casagrande, F., Gerday, C., Frère, J.-M. and Ghuysen, J.-M. The complete amino acid sequence of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces albus G. Eur. J. Biochem. 130 (1983) 53–69. [DOI] [PMID: 6825689]
3.  Ghuysen, J.-M., Frère, J.-M., Leyh-Bouille, M., Nguyen-Distèche, M., Coyette, J., Dusart, J., Joris, B., Duez, C., Dideberg, O., Charlier, P., Dive, G. and Lamotte-Brasseur, J. Bacterial wall peptidoglycan, DD-peptidases and β-lactam antibiotics. Scand. J. Infect. Dis. Suppl. 42 (1984) 17–37. [PMID: 6597561]
[EC 3.4.17.14 created 1992]
 
 
EC 3.4.17.15     
Accepted name: carboxypeptidase A2
Reaction: Similar to that of carboxypeptidase A (EC 3.4.17.1), but with a preference for bulkier C-terminal residues
Other name(s): CPA2
Comments: Isolated from rat pancreas but not present in cattle pancreas. In peptidase family M14 (carboxypeptidase A family).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 181186-98-1
References:
1.  Gardell, S.J., Craik, C.S., Clauser, E., Goldsmith, E.J., Stewart, C.B., Graf, M. and Rutter, W.J. A novel rat carboxypeptidase, CPA2: characterization, molecular cloning, and evolutionary implications on substrate specificity in the carboxypeptidase gene family. J. Biol. Chem. 263 (1988) 17828–17836. [PMID: 3182871]
[EC 3.4.17.15 created 1992]
 
 
EC 3.4.17.16     
Accepted name: membrane Pro-Xaa carboxypeptidase
Reaction: Release of a C-terminal residue other than proline, by preferential cleavage of a prolyl bond
Other name(s): carboxypeptidase P; microsomal carboxypeptidase; membrane Pro-X carboxypeptidase
Comments: One of the renal brush border exopeptidases
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9075-64-3
References:
1.  Dehm, P. and Nordwig, A. The cleavage of prolyl peptides by kidney peptidases. Isolation of a microsomal carboxypeptidase from swine kidney. Eur. J. Biochem. 17 (1970) 372–377. [DOI] [PMID: 5500406]
2.  Booth, A.G., Hubbard, L.M.L. and Kenny, A.J. Proteins of the kidney microvillar membrane. Immunoelectrophoretic analysis of the membrane hydrolase: identification and resolution of the detergent- and proteinase-solubilized forms. Biochem. J. 179 (1979) 397–405. [PMID: 486090]
3.  Hedeager-Sorensen, S. and Kenny, A.J. Proteins of the kidney microvillar membrane. Purification and properties of carboxypeptidase P from pig kidneys. Biochem. J. 229 (1985) 251–257. [PMID: 4038259]
[EC 3.4.17.16 created 1992]
 
 
EC 3.4.17.17     
Accepted name: tubulinyl-Tyr carboxypeptidase
Reaction: Cleavage of the -Glu┼Tyr bond to release the C-terminal tyrosine residue from the native tyrosinated tubulin. Inactive on Z-Glu-Tyr
Other name(s): carboxypeptidase-tubulin; soluble carboxypeptidase; tubulin-tyrosine carboxypeptidase; tubulin carboxypeptidase; tubulinyltyrosine carboxypeptidase; tyrosinotubulin carboxypeptidase; tyrosyltubulin carboxypeptidase; TTCPase; brain I carboxypeptidase; carboxypeptidase 1; CCP1
Comments: Active at neutral pH, from brain
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 73050-23-4
References:
1.  Argaraña, C.E., Barra, H.S. and Caputto, R. Tubulinyl-tyrosine carboxypeptidase from chicken brain: properties and partial purification. J. Neurochem. 34 (1980) 114–118. [DOI] [PMID: 7452228]
2.  Kumar, N. and Flavin, M. Preferential action of a brain detyrosinolating carboxypeptidase on polymerized tubulin. J. Biol. Chem. 256 (1981) 7678–7686. [DOI] [PMID: 6114100]
3.  Arce, C.A. and Barra, H.S. Association of tubulinyl-tyrosine carboxypeptidase with microtubules. FEBS Lett. 157 (1983) 75–78. [DOI] [PMID: 6862022]
4.  Berezniuk, I., Lyons, P.J., Sironi, J.J., Xiao, H., Setou, M., Angeletti, R.H., Ikegami, K. and Fricker, L.D. Cytosolic carboxypeptidase 5 removes α- and γ-linked glutamates from tubulin. J. Biol. Chem. 288 (2013) 30445–30453. [PMID: 24022482]
[EC 3.4.17.17 created 1992]
 
 
EC 3.4.17.18     
Accepted name: carboxypeptidase T
Reaction: Releases a C-terminal residue, which may be hydrophobic or positively charged
Other name(s): CPT (ambiguous)
Comments: Known from Thermoactinomyces vulgaris. In peptidase family M14 (carboxypeptidase A family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 89623-65-4
References:
1.  Osterman, A.L., Stepanov, V.M., Rudenskaya, G.N., Khodova, O.M., Tsaplina, I.A., Yakovleva, M.B. and Loginova, L.G. Carboxypeptidase T - an extracellular carboxypeptidase of thermophilic actinomycetes - a remote analog of animal carboxypeptidases. Biochemistry (USSR) 49 (1984) 292–301. [PMID: 6424730]
2.  Smulevitch, S.V., Osterman, A.L., Galperina, O.V., Matz, M.V., Zagnitko, O.P., Kadyrov, R.M., Tsaplina, I.A., Grishin, N.V., Chestukhina, G.G. and Stepanov, V.M. Molecular cloning and primary structure of Thermoactinomyces vulgaris carboxypeptidase T: a metalloenzyme endowed with dual substrate specificity. FEBS Lett. 291 (1991) 75–78. [DOI] [PMID: 1936254]
3.  Teplyakov, A., Polyakov, K., Obmolova, G., Strokopytov, B., Kuranova, I., Osterman, A., Grishin, N., Smulevitch, S., Zagnitko, O., Galperina, O., Matz, M. and Stepanov, V. Crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris. Eur. J. Biochem. 208 (1992) 281–288. [DOI] [PMID: 1521526]
[EC 3.4.17.18 created 1993]
 
 
EC 3.4.17.19     
Accepted name: carboxypeptidase Taq
Reaction: Release of a C-terminal amino acid with broad specificity, except for -Pro
Comments: A 56-kDa enzyme from Thermus aquaticus. Most active at 80° C. Type example of peptidase family M32
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9031-98-5
References:
1.  Lee, S.-H., Minagawa, E., Taguchi, H., Matsuzawa, H., Ohta, T., Kaminogawa, S. and Yamauchi, K. Purification and characterization of a thermostable carboxypeptidase (carboxypeptidase Taq) from Thermus aquaticus YT-1. Biosci. Biotechnol. Biochem. 56 (1992) 1839–1844. [DOI] [PMID: 1369078]
2.  Lee, S.-H., Taguchi, H., Yoshimura, E., Minagawa, E., Kaminogawa, S., Ohta, T. and Matsuzawa, H. Carboxypeptidase Taq, a thermostable zinc enzyme, from Thermus aquaticus YT-1: molecular cloning, sequencing, and expression of the encoding gene in Escherichia coli. Biosci. Biotechnol. Biochem. 58 (1994) 1490–1495. [DOI] [PMID: 7765282]
[EC 3.4.17.19 created 1996]
 
 
EC 3.4.17.20     
Accepted name: carboxypeptidase U
Reaction: Release of C-terminal Arg and Lys from a polypeptide
Other name(s): arginine carboxypeptidase; carboxypeptidase R; plasma carboxypeptidase B (misleading, since the term carboxypeptidase B is used for other enzymes); thrombin-activatable fibrinolysis inhibitor
Comments: Pro-carboxypeptidase U in (human) plasma is activated by thrombin or plasmin during clotting to form the unstable carboxypeptidase U, with activity similar to that of the more stable lysine carboxypeptidase, except that no preference is shown for Lys over Arg. A zinc enzyme, in peptidase family M14 (carboxypeptidase A family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 156621-18-0
References:
1.  Eaton, D.L., Malloy, B.E., Tsai, S.P., Henzel, W. and Drayna, D. Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma. J. Biol. Chem. 266 (1991) 21833–21838. [PMID: 1939207]
2.  Shinohara, T., Sakurada, C., Suzuki, T., Takeuchi, O., Campbell, W., Ikeda, S., Okada, N. and Okada, H. Pro-carboxypeptidase R cleaves bradykinin following activation. Int. Arch. Allergy Immunol. 103 (1994) 400–404. [DOI] [PMID: 8130654]
3.  Wang, W., Hendriks, D.F. and Scharpé, S. Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen. J. Biol. Chem. 269 (1994) 15937–15944. [PMID: 8195249]
4.  Tan, A.K. and Eaton, D.L. Activation and characterization of procarboxypeptidase B from human plasma. Biochemistry 34 (1995) 5811–5816. [PMID: 7727441]
5.  Broze, G.J., Jr. and Higuchi, D.A. Coagulation-dependent inhibition of fibrinolysis: Role of carboxypeptidase U and the premature lysis of clots from hemophilic plasma. Blood 88 (1996) 3815–3823. [PMID: 8916945]
[EC 3.4.17.20 created 1997]
 
 
EC 3.4.17.21     
Accepted name: glutamate carboxypeptidase II
Reaction: Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-γ-glutamates
Glossary: quisqualic acid = 3-(3,5-dioxo-1,2,4-oxazadiazolidin-2-yl)Ala
Other name(s): N-acetylated-γ-linked-acidic dipeptidase (NAALADase); folate hydrolase; prostate-specific membrane antigen; pteroylpoly-γ-glutamate carboxypeptidase; microsomal γ-glutamyl carboxypeptidase; pteroylpolyglutamate hydrolase; folylpolyglutamate hydrolase; pteroylpoly-γ-glutamate hydrolase; pteroylpolygammaglutamyl hydrolase; pteroylpolyglutamic acid hydrolase; PSM antigen; acetylaspartylglutamate dipeptidase; NAALA dipeptidase; rat NAAG peptidase; mGCP; membrane glutamate carboxypeptidase; N-acetylated-α-linked-amino dipeptidase; prostrate-specific membrane antigen; N-Acetylated α-linked acidic dipeptidase; PSMA
Comments: A metallo-carboxypeptidase that is predominantly expressed as a membrane-bound enzyme of 94-100 kDa , but also exists in a soluble form. Hydrolyses α-peptide bonds in Ac-Asp-Glu, Asp-Glu, and Glu-Glu, but also γ-glutamyl bonds in γ-Glu-Glu, and folylpoly-γ-glutamates. With folylpoly-γ-glutamates, shows processive carboxypeptidase activity to produce pteroylmonoglutamate [4]. Does not hydrolyse Ac-β-Asp-Glu. Known inhibitors: quisqualic acid, Ac-β-Asp-Glu, and 2-phosphonomethyl-pentanedioate. In peptidase family M28 of Vibrio leucyl aminopeptidase. The release of C-terminal glutamate from folylpoly-γ-glutamates is also catalysed by EC 3.4.17.11 (glutamate carboxypeptidase) and EC 3.4.19.9 (folate γ-glutamyl hydrolase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9074-87-7
References:
1.  Heston, W.D.W. Characterization and glutamyl preferring carboxypeptidase function of prostate specific membrane antigen: a novel folate hydrolase. Urology 49 (1997) 104–112. [PMID: 9123729]
2.  Rawlings, N.D. and Barrett, A.J. Structure of membrane glutamate carboxypeptidase. Biochim. Biophys. Acta 1339 (1997) 247–252. [DOI] [PMID: 9187245]
3.  Halsted, C.H., Ling, E.-H., Luthi-Carter, R., Villanueva, J.A., Gardner, J.M., Coyle, J.T. Folylpoly-γ-glutamate carboxypeptidase from pig jejunum: molecular characterization and relation to glutamate carboxypeptidase II. J. Biol. Chem. 273 (1998) 20417–20424. [DOI] [PMID: 9685395]
4.  Luthi-Carter, R., Berger, U.V., Barczak, A.K., Enna, M. and Coyle, J.T. Isolation and expression of a rat brain cDNA encoding glutamate carboxypeptidase II. Proc. Natl. Acad. Sci. USA 95 (1998) 3215–3220. [DOI] [PMID: 9501243]
[EC 3.4.17.21 created 1997, modified 2000 (EC 3.4.13.8 created 1972 and EC 3.4.19.8 created 1992, incorporated 2000)]
 
 
EC 3.4.17.22     
Accepted name: metallocarboxypeptidase D
Reaction: Releases C-terminal Arg and Lys from polypeptides
Other name(s): carboxypeptidase D (cattle, human, mouse, rat); gp180 (duck)
Comments: Activated by Co2+; inhibited by [(2-guanidinoethyl)sulfanyl]butanedioate. Large molecule (180 kDa) because of presence of three copies of metallopeptidase domain. The product of the silver gene (Drosophila) is similar. A zinc metallopeptidase in peptidase family M14 (carboxypeptidase A family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 153967-26-1
References:
1.  Kuroki, K., Eng, F., Ishikawa, T., Turck, C., Harada, F. and Ganem, D. gp180, a host cell glycoprotein that binds duck hepatitis B virus particles, is encoded by a member of the carboxypeptidase gene family. J. Biol. Chem. 270 (1995) 15022–15028. [DOI] [PMID: 9525948]
2.  Song, L.X. and Fricker, L.D. Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme, from bovine pituitary. J. Biol. Chem. 270 (1995) 25007–25013. [DOI] [PMID: 7559630]
3.  Song, L.X. and Fricker, L.D. Tissue distribution and characterization of soluble and membrane-bound forms of metallocarboxypeptidase D. J. Biol. Chem. 271 (1996) 28884–28889. [DOI] [PMID: 8910535]
[EC 3.4.17.22 created 1997]
 
 


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