The Enzyme Database

Displaying entries 51-100 of 548.

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EC 3.4.11.12      
Deleted entry:  thermophilic aminopeptidase
[EC 3.4.11.12 created 1978, deleted 1997]
 
 
EC 3.4.11.13     
Accepted name: clostridial aminopeptidase
Reaction: Release of any N-terminal amino acid, including proline and hydroxyproline, but no cleavage of Xaa-Pro-
Other name(s): Clostridium histolyticum aminopeptidase
Comments: A secreted enzyme from Clostridium histolyticum, requiring Mn2+ or Co2+
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 59680-69-2
References:
1.  Kessler, E. and Yaron, A. A novel aminopeptidase from Clostridium histolyticum. Biochem. Biophys. Res. Commun. 50 (1973) 405–412. [DOI] [PMID: 4631895]
2.  Kessler, E. and Yaron, A. An extracellular aminopeptidase from Clostridium histolyticum. Eur. J. Biochem. 63 (1976) 271–287. [DOI] [PMID: 4318]
3.  Kessler, E. and Yaron, A. Extracellular aminopeptidase from Clostridium histolyticum. Methods Enzymol. 45 (1976) 544–552. [DOI] [PMID: 13266]
[EC 3.4.11.13 created 1978]
 
 
EC 3.4.11.14     
Accepted name: cytosol alanyl aminopeptidase
Reaction: Release of an N-terminal amino acid, preferentially alanine, from a wide range of peptides, amides and arylamides
Other name(s): arylamidase; aminopolypeptidase; thiol-activated aminopeptidase; human liver aminopeptidase; puromycin-sensitive aminopeptidase; soluble alanyl aminopeptidase; cytosol aminopeptidase III; alanine aminopeptidase
Comments: A puromycin-sensitive, Co2+-activated zinc-sialoglycoprotein that is generally cytosolic. Multiple forms are widely distributed in mammalian tissues and body fluids. In peptidase family M1 (membrane alanyl aminopeptidase family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 243859-94-1
References:
1.  Starnes, W.L. and Behal, F.J. A human liver aminopeptidase. The amino acid and carbohydrate content, and some physical properties of a sialic acid containing glycoprotein. Biochemistry 13 (1974) 3221–3227. [PMID: 4841062]
2.  Kao, Y.J., Starnes, W.L. and Behal, F.J. Human kidney alanine aminopeptidase: physical and kinetic properties of a sialic acid containing glycoprotein. Biochemistry 17 (1978) 2990–2994. [PMID: 698181]
3.  Sidorowicz, W., Hsia, W.-C., Maslej-Zownir, M. and Behal, F.J. Multiple molecular forms of human alanine aminopeptidase: imunochemical properties. Clin. Chim. Acta 107 (1980) 245–256. [DOI] [PMID: 6108169]
[EC 3.4.11.14 created 1978]
 
 
EC 3.4.11.15     
Accepted name: aminopeptidase Y
Reaction: Preferentially, release of N-terminal lysine
Other name(s): aminopeptidase Co; aminopeptidase (cobalt-activated); lysyl aminopeptidase
Comments: Requires Co2+; inhibited by Zn2+ and Mn2+. An enzyme best known from Saccharomyces cerevisiae that hydrolyses Lys-NHPhNO2 and, more slowly, Arg-NHPhNO2. Type example of peptidase family M28
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 114796-97-3
References:
1.  Achstetter, T., Ehmann, C. and Wolf, D.H. Aminopeptidase Co, a new yeast peptidase. Biochem. Biophys. Res. Commun. 109 (1982) 341–347. [DOI] [PMID: 6758786]
2.  Yasuhara, T., Nakai, T. and Ohashi, A. Aminopeptidase Y, a new aminopeptidase from Saccharomyces cerevisiae. Purification, properties, localization, and processing by protease B. J. Biol. Chem. 269 (1994) 13644–13650. [PMID: 8175799]
3.  Nishizawa, M., Yasuhara, T., Nakai, T., Fujiki, Y. and Ohashi, A. Molecular cloning of the aminopeptidase Y gene of Saccharomyces cerevisiae. Sequence analysis and gene disruption of a new aminopeptidase. J. Biol. Chem. 269 (1994) 13651–13655. [PMID: 8175800]
[EC 3.4.11.15 created 1989, modified 1997]
 
 
EC 3.4.11.16     
Accepted name: Xaa-Trp aminopeptidase
Reaction: Release of a variety of N-terminal residues (especially glutamate and leucine) from peptides, provided tryptophan (or at least phenylalanine or tyrosine) is the penultimate residue. Also acts on Glu┼Trp, Leu┼Trp and a number of other dipeptides
Other name(s): aminopeptidase W; aminopeptidase X-Trp; X-Trp aminopeptidase
Comments: A glycoprotein containing Zn2+, from renal and intestinal brush border membranes
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 137010-33-4
References:
1.  Gee, N.S. and Kenny, A.J. Proteins of the kidney microvillar membrane. The 130kDa protein in pig kidney, recognised by monoclonal antibody GK5C1, is an ectoenzyme with aminopeptidase activity. Biochem. J. 230 (1985) 753–764. [PMID: 4062876]
2.  Gee, N.S. and Kenny, A.J. Proteins of the kidney microvillar membrane. Enzymic and molecular properties of aminopeptidase W. Biochem. J. 246 (1987) 97–102. [PMID: 2890346]
[EC 3.4.11.16 created 1989]
 
 
EC 3.4.11.17     
Accepted name: tryptophanyl aminopeptidase
Reaction: Preferential release of N-terminal tryptophan
Other name(s): tryptophan aminopeptidase; L-tryptophan aminopeptidase
Comments: From Trichosporon cutaneum. Also acts on L-tryptophanamide. Requires Mn2+
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 76689-19-5
References:
1.  Iwayama, A., Kimura, T., Adachi, O. and Ameyama, M. Crystallization and characterization of a novel aminopeptidase from Trichosporon cutaneum. Agric. Biol. Chem. 47 (1983) 2483–2493.
[EC 3.4.11.17 created 1989]
 
 
EC 3.4.11.18     
Accepted name: methionyl aminopeptidase
Reaction: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides
Other name(s): methionine aminopeptidase; peptidase M; L-methionine aminopeptidase; MAP
Comments: This membrane-bound enzyme, which is present in both prokaryotes and eukaryotes, releases the initiator methionine from nascent peptides. The activity is dependent on the identity of the second, third and fourth amino acid residues of the target protein, but in general the enzyme acts only when the penultimate residue is small and uncharged (e.g. Gly, Ala, Cys, Ser, Thr, and Val).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 61229-81-0
References:
1.  Yoshida, A. and Lin, M. NH2-terminal formylmethionine- and NH2-terminal methionine-cleaving enzymes in rabbits. J. Biol. Chem. 247 (1972) 952–957. [PMID: 4110013]
2.  Tsunasawa, S., Stewart, J.W. and Sherman, F. Acylamino acid-releasing enzyme from rat liver. J. Biol. Chem. 260 (1985) 5832. [PMID: 2985590]
3.  Freitas, J.O., Jr., Termignoni, C. and Guimaraes, J.A. Methionine aminopeptidase associated with liver mitochondria and microsomes. Int. J. Biochem. 17 (1985) 1285–1291. [PMID: 3937747]
4.  Ben-Bassat, A., Bauer, K., Chang, S.-Y., Myambo, K., Boosman, A. and Chang, S. Processing of the initiation methionine from proteins: properties of Escherichia coli methionine aminopeptidase and its gene structure. J. Bacteriol. 169 (1987) 751–757. [DOI] [PMID: 3027045]
5.  Roderick, S.L. and Matthews, B.W. Crystallization of methionine aminopeptidase from Escherichia coli. J. Biol. Chem. 263:16531 (1988). [PMID: 3141408]
[EC 3.4.11.18 created 1990]
 
 
EC 3.4.11.19     
Accepted name: D-stereospecific aminopeptidase
Reaction: Release of an N-terminal D-amino acid from a peptide, Xaa┼Yaa-, in which Xaa is preferably D-Ala, D-Ser or D-Thr. D-Amino acid amides and methyl esters also are hydrolysed, as is glycine amide
Other name(s): D-aminopeptidase
Comments: Known from the bacterium Ochrobactrum anthropi. In peptidase family S12 (D-Ala-D-Ala carboxypeptidase family) [2]
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 57534-78-8
References:
1.  Asano, Y., Nakazawa, A., Kato, Y. and Kondo, K. Properties of a novel D-stereospecific aminopeptidase from Ochrobactrum anthropi. J. Biol. Chem. 264 (1989) 14233–14239. [PMID: 2760064]
2.  Asano, Y., Kato, Y., Yamada, A. and Kondo, K. Structural similarity of D-aminopeptidase to carboxypeptidase DD and β-lactamases. Biochemistry 31 (1992) 2316–2328. [PMID: 1540587]
[EC 3.4.11.19 created 1993]
 
 
EC 3.4.11.20     
Accepted name: aminopeptidase Ey
Reaction: Differs from other aminopeptidases in broad specificity for amino acids in the P1 position and the ability to hydrolyse peptides of four or five residues that contain Pro in the P1′ position
Comments: A zinc glycoprotein in peptidase family M1 (membrane alanyl aminopeptidase family), composed of two 150 kDa subunits. From the plasma fraction of hen egg yolk
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 9031-94-1
References:
1.  Ichishima, E., Yamagata, Y., Chiba, H., Sawaguchi, K. and Tanaka, T. Soluble and bound forms of aminopeptidase in hens egg-yolk. Agric. Biol. Chem. 53 (1989) 1867–1872.
2.  Tanaka, T. and Ichishima, E. Substrate specificity of aminopeptidase Ey from hen's egg yolk. Comp. Biochem. Physiol. [B] 105 (1993) 105–110. [PMID: 7684960]
3.  Tanaka, T. and Ichishima, E. Molecular properties of aminopeptidase Ey as a zinc-metalloenzyme. Int. J. Biochem. 25 (1993) 1681–1688. [PMID: 8288037]
[EC 3.4.11.20 created 1995]
 
 
EC 3.4.11.21     
Accepted name: aspartyl aminopeptidase
Reaction: Release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate
Comments: Aminoacyl-arylamides are poor substrates. This is an abundant cytosolic enzyme in mammalian cells, in peptidase family M18 of aminopeptidase I
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 9074-83-3
References:
1.  Kelly, J.A., Neidle, E.L. and Neidle, A. An aminopeptidase from mouse brain cytosol that cleaves N-terminal acidic amino acid residues. J. Neurochem. 40 (1983) 1727–1734. [DOI] [PMID: 6854330]
2.  Wilk, S., Wilk, E. and Magnusson, R.P. Purification, characterization and cloning of a cytosolic aspartyl aminopeptidase. J. Biol. Chem. 273 (1998) 15961–15970. [DOI] [PMID: 9632644]
[EC 3.4.11.21 created 2000]
 
 
EC 3.4.11.22     
Accepted name: aminopeptidase I
Reaction: Release of an N-terminal amino acid, preferably a neutral or hydrophobic one, from a polypeptide. Aminoacyl-arylamides are poor substrates
Other name(s): aminopeptidase III; aminopeptidase yscI; leucine aminopeptidase IV; yeast aminopeptidase I
Comments: A 640-kDa, dodecameric enzyme best known as the major vacuolar aminopeptidase of yeast, Saccharomyces cervisiae, in which species it was first given the name aminopeptidase I (one), amongst others. Activity is stimulated by both Zn2+ and Cl- ions. Type example of peptidase family M18
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 9031-94-1
References:
1.  Johnson, M.J. Isolation and properties of a pure yeast polypeptidase. J. Biol. Chem. 137 (1941) 575–586.
2.  Metz, G. and Rohm, K.-H. Yeast aminopeptidase I. Chemical composition and catalytic properties. Biochim. Biophys. Acta 429 (1976) 933–949. [DOI] [PMID: 5147]
3.  Chang, Y-H. and Smith, J.A. Molecular cloning and sequencing of genomic DNA encoding aminopeptidase I from Saccharomyces cerevisiae. J. Biol. Chem. 264 (1989) 6979–6983. [PMID: 2651436]
4.  Oda, M.N., Scott, S.V., Hefner-Gravink, A., Caffarelli, A.D. and Klionsky, D.J. Identification of a cytoplasm to vacuole targeting determinant in aminopeptidase I. J. Cell Biol. 132 (1996) 999–1010. [PMID: 8601598]
[EC 3.4.11.22 created 1997]
 
 
EC 3.4.11.23     
Accepted name: PepB aminopeptidase
Reaction: Release of an N-terminal amino acid, Xaa, from a peptide or arylamide. Xaa is preferably Glu or Asp but may be other amino acids, including Leu, Met, His, Cys and Gln
Other name(s): Salmonella enterica serovar Typhimurium peptidase B
Comments: A 270-kDa protein composed of six 46.3-kDa subunits. The pH optimum is in the alkaline range and activity is stimulated by KCl. In peptidase family M17.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, SWISSPROT, CAS registry number: 928346-44-5
References:
1.  Mathew, Z., Knox, T.M. and Miller, C.G. Salmonella enterica serovar typhimurium peptidase B is a leucyl aminopeptidase with specificity for acidic amino acids. J. Bacteriol. 182 (2000) 3383–3393. [DOI] [PMID: 10852868]
[EC 3.4.11.23 created 2003]
 
 
EC 3.4.11.24     
Accepted name: aminopeptidase S
Reaction: Release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
Other name(s): Mername-AA022 peptidase; SGAP; aminopeptidase (Streptomyces griseus); Streptomyces griseus aminopeptidase; S. griseus AP; double-zinc aminopeptidase
Comments: Aminopeptidases are associated with many biological functions, including protein maturation, protein degradation, cell-cycle control and hormone-level regulation [3,4]. This enzyme contains two zinc molecules in its active site and is activated by Ca2+ [4]. In the presence of Ca2+, the best substrates are Leu-Phe, Leu-Ser, Leu-pNA (aminoacyl-p-nitroanilide), Phe-Phe-Phe and Phe-Phe [3]. Peptides with proline in the P1′ position are not substrates [3]. Belongs in peptidase family M28.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Spungin, A. and Blumberg, S. Streptomyces griseus aminopeptidase is a calcium-activated zinc metalloprotein. Purification and properties of the enzyme. Eur. J. Biochem. 183 (1989) 471–477. [DOI] [PMID: 2503378]
2.  Ben-Meir, D., Spungin, A., Ashkenazi, R. and Blumberg, S. Specificity of Streptomyces griseus aminopeptidase and modulation of activity by divalent metal ion binding and substitution. Eur. J. Biochem. 212 (1993) 107–112. [DOI] [PMID: 8444149]
3.  Arima, J., Uesugi, Y., Iwabuchi, M. and Hatanaka, T. Study on peptide hydrolysis by aminopeptidases from Streptomyces griseus, Streptomyces septatus and Aeromonas proteolytica. Appl. Microbiol. Biotechnol. 70 (2006) 541–547. [DOI] [PMID: 16080009]
4.  Fundoiano-Hershcovitz, Y., Rabinovitch, L., Langut, Y., Reiland, V., Shoham, G. and Shoham, Y. Identification of the catalytic residues in the double-zinc aminopeptidase from Streptomyces griseus. FEBS Lett. 571 (2004) 192–196. [DOI] [PMID: 15280041]
5.  Gilboa, R., Greenblatt, H.M., Perach, M., Spungin-Bialik, A., Lessel, U., Wohlfahrt, G., Schomburg, D., Blumberg, S. and Shoham, G. Interactions of Streptomyces griseus aminopeptidase with a methionine product analogue: a structural study at 1.53 Å resolution. Acta Crystallogr. D Biol. Crystallogr. 56 (2000) 551–558. [PMID: 10771423]
[EC 3.4.11.24 created 2008]
 
 
EC 3.4.11.25     
Accepted name: β-peptidyl aminopeptidase
Reaction: Cleaves N-terminal β-homoamino acids from peptides composed of 2 to 6 amino acids
Other name(s): BapA (ambiguous)
Comments: Sphingosinicella xenopeptidilytica strain 3-2W4 is able to utilize the β-peptides β-homoVal-β-homoAla-β-homoLeu and β-homoAla-β-homoLeu as sole carbon and energy sources [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Heck, T., Limbach, M., Geueke, B., Zacharias, M., Gardiner, J., Kohler, H.P. and Seebach, D. Enzymatic degradation of β- and mixed α,β-oligopeptides. Chem. Biodivers. 3 (2006) 1325–1348. [DOI] [PMID: 17193247]
2.  Geueke, B., Namoto, K., Seebach, D. and Kohler, H.P. A novel β-peptidyl aminopeptidase (BapA) from strain 3-2W4 cleaves peptide bonds of synthetic β-tri- and β-dipeptides. J. Bacteriol. 187 (2005) 5910–5917. [DOI] [PMID: 16109932]
3.  Geueke, B., Heck, T., Limbach, M., Nesatyy, V., Seebach, D. and Kohler, H.P. Bacterial β-peptidyl aminopeptidases with unique substrate specificities for β-oligopeptides and mixed β,α-oligopeptides. FEBS J. 273 (2006) 5261–5272. [DOI] [PMID: 17064315]
4.  Heck, T., Kohler, H.P., Limbach, M., Flögel, O., Seebach, D. and Geueke, B. Enzyme-catalyzed formation of β-peptides: β-peptidyl aminopeptidases BapA and DmpA acting as β-peptide-synthesizing enzymes. Chem. Biodivers. 4 (2007) 2016. [DOI] [PMID: 17886858]
[EC 3.4.11.25 created 2011]
 
 
EC 3.4.11.26     
Accepted name: intermediate cleaving peptidase 55
Reaction: The enzyme cleaves the Pro36-Pro37 bond of cysteine desulfurase (EC 2.8.1.7) removing three amino acid residues (Tyr-Ser-Pro) from the N-terminus after cleavage by mitochondrial processing peptidase.
Other name(s): Icp55; mitochondrial intermediate cleaving peptidase 55 kDa
Comments: Icp55 removes the destabilizing N-terminal amino acid residues that are left after cleavage by the mitochondrial processing peptidase, leading to the stabilisation of the substrate. The enzyme can remove single amino acids or a short peptide, as in the case of cysteine desulfurase (EC 2.8.1.7), where three amino acids are removed.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS
References:
1.  Naamati, A., Regev-Rudzki, N., Galperin, S., Lill, R. and Pines, O. Dual targeting of Nfs1 and discovery of its novel processing enzyme, Icp55. J. Biol. Chem. 284 (2009) 30200–30208. [DOI] [PMID: 19720832]
2.  Vogtle, F.N., Wortelkamp, S., Zahedi, R.P., Becker, D., Leidhold, C., Gevaert, K., Kellermann, J., Voos, W., Sickmann, A., Pfanner, N. and Meisinger, C. Global analysis of the mitochondrial N-proteome identifies a processing peptidase critical for protein stability. Cell 139 (2009) 428–439. [DOI] [PMID: 19837041]
[EC 3.4.11.26 created 2011]
 
 
EC 3.4.12.1      
Transferred entry: now EC 3.4.16.5 (carboxypeptidase C) and EC 3.4.16.6 (carboxypeptidase D)
[EC 3.4.12.1 created 1972, deleted 1978]
 
 
EC 3.4.12.2      
Transferred entry: now EC 3.4.17.1, carboxypeptidase A
[EC 3.4.12.2 created 1972, deleted 1978]
 
 
EC 3.4.12.3      
Transferred entry: now EC 3.4.17.2, carboxypeptidase B
[EC 3.4.12.3 created 1972, deleted 1978]
 
 
EC 3.4.12.4      
Transferred entry: now EC 3.4.16.2, lysosomal Pro-Xaa carboxypeptidase
[EC 3.4.12.4 created 1972, modified 1976, deleted 1978]
 
 
EC 3.4.12.5      
Transferred entry: now EC 3.5.1.28, N-acetylmuramoyl-L-alanine amidase
[EC 3.4.12.5 created 1972, deleted 1978]
 
 
EC 3.4.12.6      
Transferred entry: now EC 3.4.17.8, muramoyl-pentapeptidase carboxypeptidase
[EC 3.4.12.6 created 1972, deleted 1978]
 
 
EC 3.4.12.7      
Transferred entry: now EC 3.4.17.3, lysine carboxypeptidase
[EC 3.4.12.7 created 1972, deleted 1978]
 
 
EC 3.4.12.8      
Transferred entry: now EC 3.4.17.4, Gly-Xaa carboxypeptidase
[EC 3.4.12.8 created 1972, deleted 1978]
 
 
EC 3.4.12.9      
Deleted entry: aspartate carboxypeptidase
[EC 3.4.12.9 created 1972, deleted 1978]
 
 
EC 3.4.12.10      
Transferred entry: now EC 3.4.19.9, γ-glutamyl hydrolase
[EC 3.4.12.10 created 1972, modified 1976, deleted 1978]
 
 
EC 3.4.12.11      
Transferred entry: now EC 3.4.17.6, alanine carboxypeptidase
[EC 3.4.12.11 created 1972, deleted 1978]
 
 
EC 3.4.12.12      
Transferred entry: now EC 3.4.16.5 (carboxypeptidase C) and EC 3.4.16.6 (carboxypeptidase D)
[EC 3.4.12.12 created 1972, deleted 1978]
 
 
EC 3.4.12.13      
Deleted entry: γ-glutamylglutamate carboxypeptidase
[EC 3.4.12.13 created 1975, modified 1976, deleted 1978]
 
 
EC 3.4.13.1      
Transferred entry: glycyl-glycine dipeptidase. Now EC 3.4.13.18, cytosol nonspecific dipeptidase
[EC 3.4.13.1 created 1972, deleted 1978 [transferred to EC 3.4.13.11, deleted 1992]]
 
 
EC 3.4.13.2      
Transferred entry: glycyl-leucine dipeptidase. Now EC 3.4.13.18, cytosol nonspecific dipeptidase
[EC 3.4.13.2 created 1972, deleted 1978 [transferred to EC 3.4.13.11, deleted 1992]]
 
 
EC 3.4.13.3      
Deleted entry: Xaa-His dipeptidase. The activity is covered by EC 3.4.13.18, cytosol nonspecific dipeptidase and EC 3.4.13.20, β-Ala-His dipeptidase.
[EC 3.4.13.3 created 1961 as EC 3.4.3.3, transferred 1972 to EC 3.4.13.3, modified 1989 (EC 3.4.13.13 created 1981, incorporated 1992), deleted 2011]
 
 
EC 3.4.13.4     
Accepted name: Xaa-Arg dipeptidase
Reaction: Preferential hydrolysis of Xaa┼Arg, Xaa┼Lys or Xaa┼ornithine dipeptides
Other name(s): aminoacyl-lysine dipeptidase; N2-(4-amino-butyryl)-L-lysine hydrolase; X-Arg dipeptidase
Comments: Widely distributed in mammals
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-72-5
References:
1.  Kumon, A., Matsuoka, Y., Kakimoto, Y., Nakajima, T. and Sano, I. A peptidase that hydrolyzes α-N-(γ-aminobutyryl)lysine. Biochim. Biophys. Acta 200 (1970) 466–474. [DOI] [PMID: 5436646]
[EC 3.4.13.4 created 1972]
 
 
EC 3.4.13.5     
Accepted name: Xaa-methyl-His dipeptidase
Reaction: Hydrolysis of anserine (β-alanyl┼Nπ-methyl-L-histidine), carnosine, homocarnosine, glycyl┼leucine and other dipeptides with broad specificity
Other name(s): anserinase; aminoacyl-methylhistidine dipeptidase; acetylhistidine deacetylase; N-acetylhistidine deacetylase; α-N-acetyl-L-histidine aminohydrolase; X-methyl-His dipeptidase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9027-38-7
References:
1.  Jones, N.R. The free amino acids of fish. 1-Methylhistidine and β-alanine liberation by skeletal muscle anserinase of codling (Gadus callarias). Biochem. J. 60 (1955) 81–87. [PMID: 14363188]
2.  Baslow, M.H. and Lenney, J.F. α-N-Acetyl-L-histidine amidohydrolase activity from the brain of the skipjack tuna Katsuwonus pelamis. Can. J. Biochem. 45 (1967) 337–340. [PMID: 6067033]
3.  Lenney, J.F., Baslow, M.H. and Sugiyama, G.H. Similarity of tuna N-acetylhistidine deacetylase and cod fish anserinase. Comp. Biochem. Physiol. B Comp. Biochem. 61 (1978) 253–258. [PMID: 318374]
[EC 3.4.13.5 created 1961 as EC 3.4.3.4, transferred 1972 to EC 3.4.13.5, modified 1981 (EC 3.5.1.34 created 1972, incorporated 1981)]
 
 
EC 3.4.13.6      
Transferred entry: Cys-Gly dipeptidase. Now EC 3.4.11.2, membrane alanyl aminopeptidase
[EC 3.4.13.6 created 1961 as EC 3.4.3.5, transferred 1972 to EC 3.4.13.6]
 
 
EC 3.4.13.7     
Accepted name: Glu-Glu dipeptidase
Reaction: Hydrolysis of the Glu┼Glu dipeptide
Other name(s): α-glutamyl-glutamate dipeptidase; glutamylglutamic arylamidase
Comments: It is unclear whether the specificity of this enzyme extends to other α-glutamyl dipeptides
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37288-73-6
References:
1.  Pratt, A.G., Crawford, E.J. and Friedkin, M. The hydrolysis of mono-, di-, and triglutamate derivatives of folic acid with bacterial enzymes. J. Biol. Chem. 243 (1968) 6367–6372. [PMID: 5726892]
[EC 3.4.13.7 created 1972]
 
 
EC 3.4.13.8      
Transferred entry: Pro-X dipeptidase. Now EC 3.4.13.18, cytosol nonspecific dipeptidase
[EC 3.4.13.8 created 1961 as EC 3.4.3.6, transferred 1972 to EC 3.4.13.8]
 
 
EC 3.4.13.9     
Accepted name: Xaa-Pro dipeptidase
Reaction: Hydrolysis of Xaa┼Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-Pro
Other name(s): prolidase; imidodipeptidase; proline dipeptidase; peptidase D; γ-peptidase; X-Pro dipeptidase
Comments: A Mn2+-activated enzyme, in peptidase family M24 (methionyl aminopeptidase family); cytosolic from most animal tissues.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9025-32-5
References:
1.  Davis, N.C. and Smith, E.L. Purification and some properties of prolidase of swine kidney. J. Biol. Chem. 224 (1957) 261–275. [PMID: 13398404]
2.  Sjöström, H., Norén, O. and Josefsson, L. Purification and specificity of pig intestinal prolidase. Biochim. Biophys. Acta 327 (1973) 457–470. [DOI] [PMID: 4778946]
3.  Baksi, K. and Radhakrishnan, A.N. Purification and properties of prolidase (imidodipeptidase) from monkey small intestine. Indian J. Biochem. Biophys. 11 (1974) 7–11. [PMID: 4435812]
4.  Browne, P. and O'Cuinn, G. The purification and characterization of a proline dipeptidase from guinea pig brain. J. Biol. Chem. 258 (1983) 6147–6154. [PMID: 6853481]
[EC 3.4.13.9 created 1961 as EC 3.4.3.7, transferred 1972 to EC 3.4.13.9]
 
 
EC 3.4.13.10      
Transferred entry: β-aspartyldipeptidase. Now EC 3.4.19.5, β-aspartyl-peptidase
[EC 3.4.13.10 created 1972, deleted 1992]
 
 
EC 3.4.13.11      
Transferred entry: dipeptidase. Now EC 3.4.13.19, membrane dipeptidase
[EC 3.4.13.11 created 1972, deleted 1992]
 
 
EC 3.4.13.12     
Accepted name: Met-Xaa dipeptidase
Reaction: Hydrolysis of Met┼Xaa dipeptides
Other name(s): methionyl dipeptidase; dipeptidase M; Met-X dipeptidase
Comments: A Mn2+-activated Escherichia coli enzyme with thiol dependence
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37341-91-6
References:
1.  Brown, J.L. Purification and properties of dipeptidase M from Escherichia coli B. J. Biol. Chem. 248 (1973) 409–416. [PMID: 4567782]
[EC 3.4.13.12 created 1976]
 
 
EC 3.4.13.13      
Transferred entry: homocarnosinase. Now EC 3.4.13.3, X-His dipeptidase
[EC 3.4.13.13 created 1981, deleted 1992]
 
 
EC 3.4.13.14      
Deleted entry:  γ-glutamyldipeptidase
[EC 3.4.13.14 created 1989, deleted 1992]
 
 
EC 3.4.13.15      
Transferred entry: N2-β-alanylarginine dipeptidase. Now EC 3.4.13.18, cytosol nonspecific dipeptidase
[EC 3.4.13.15 created 1989, deleted 1992]
 
 
EC 3.4.13.16      
Deleted entry:  aspartylphenylalanine dipeptidase
[EC 3.4.13.16 created 1989, deleted 1992]
 
 
EC 3.4.13.17     
Accepted name: non-stereospecific dipeptidase
Reaction: Hydrolysis of dipeptides containing either D- or L-amino acids or both
Other name(s): peptidyl-D-amino acid hydrolase; D-(or L-)aminoacyl-dipeptidase
Comments: A digestive enzyme of cephalopods
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 90371-43-0
References:
1.  D'Aniello, A. and Strazullo, L. Peptidyl-D-amino acid hydrolase from Loligo vulgaris Lam. J. Biol. Chem. 259 (1984) 4237–4243. [PMID: 6444201]
[EC 3.4.13.17 created 1990]
 
 
EC 3.4.13.18     
Accepted name: cytosol nonspecific dipeptidase
Reaction: Hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids
Other name(s): N2-β-alanylarginine dipeptidase; glycyl-glycine dipeptidase; glycyl-leucine dipeptidase; iminodipeptidase; peptidase A; Pro-X dipeptidase; prolinase; prolyl dipeptidase; prolylglycine dipeptidase; iminodipeptidase; prolinase; L-prolylglycine dipeptidase; prolylglycine dipeptidase; diglycinase; Gly-Leu hydrolase; glycyl-L-leucine dipeptidase; glycyl-L-leucine hydrolase; glycyl-L-leucine peptidase; L-amino-acyl-L-amino-acid hydrolase; glycylleucine peptidase; glycylleucine hydrolase; glycylleucine dipeptide hydrolase; non-specific dipeptidase; human cytosolic non-specific dipeptidase; glycyl-L-leucine hydrolase; glycyl-glycine dipeptidase
Comments: A zinc enzyme with broad specificity, varying somewhat with source species. Activated and stabilized by dithiothreitol and Mn2+. Inhibited by bestatin and leucine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-31-4
References:
1.  Bauer, K. Cytosol non-specific dipeptidase. In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Ed.), Handbook of Proteolytic Enzymes, Academic Press, London, 1998, pp. 1520–1522.
[EC 3.4.13.18 created 1961 as EC 3.4.3.1 and EC 3.4.3.2, transferred 1972 to EC 3.4.13.1 and EC 3.4.13.2, transferred 1978 to EC 3.4.13.11, part transferred 1992 to EC 3.4.13.18, modified 2000 (EC 3.4.13.15 created 1989, incorporated 1992)]
 
 
EC 3.4.13.19     
Accepted name: membrane dipeptidase
Reaction: Hydrolysis of dipeptides
Other name(s): renal dipeptidase; dehydropeptidase I (DPH I); dipeptidase (ambiguous); aminodipeptidase; dipeptide hydrolase (ambiguous); dipeptidyl hydrolase (ambiguous); nonspecific dipeptidase; glycosyl-phosphatidylinositol-anchored renal dipeptidase; MDP
Comments: A membrane-bound, zinc enzyme with broad specificity. Abundant in the kidney cortex. Inhibited by bestatin and cilastatin. Type example of peptidase family M19.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9031-99-6
References:
1.  Campbell, B., Lin, H., Davis, R. and Ballew, E. The purification and properties of a particulate renal dipeptidase. Biochim. Biophys. Acta 118 (1966) 371–386. [PMID: 5961612]
2.  Campbell, B.J. Renal dipeptidase. Methods Enzymol. 19 (1970) 722–729.
3.  Kropp, H., Sundelof, J.G., Hajdu, R. and Kahan, F.M. Metabolism of thienamycin and related carbapenem antibiotics by renal dipeptidase, dehydropeptidase-I. Antimicrob. Agents Chemother. 22 (1982) 62–70. [PMID: 7125632]
4.  Hooper, N.M., Keen, J.N. and Turner, A.J. Characterization of the glycosyl-phosphatidylinositol-anchored human renal dipeptidase reveals that it is more extensively glycosylated than the pig enzyme. Biochem. J. 265 (1990) 429–433. [PMID: 2137335]
[EC 3.4.13.19 created 1961 as EC 3.4.3.1 and EC 3.4.3.2, transferred 1972 to EC 3.4.13.1 and EC 3.4.13.2, transferred 1978 to EC 3.4.13.11, part transferred 1992 to EC 3.4.13.19, modified 2011]
 
 
EC 3.4.13.20     
Accepted name: β-Ala-His dipeptidase
Reaction: Preferential hydrolysis of the β-Ala┼His dipeptide (carnosine), and also anserine, Xaa┼His dipeptides and other dipeptides including homocarnosine
Other name(s): serum carnosinase
Comments: Present in the serum of humans and higher primates, but not in the serum of other mammals. Activated by Cd2+ and citrate. Belongs in peptidase family M20.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 525589-43-9
References:
1.  Lenney, J.F., George, R.P., Weiss, A.M., Kucera, C.M., Chan, P.W.H. and Rinzler, G.S. Human serum carnosinase: characterization, distinction from cellular carnosinase, and activation by cadmium. Clin. Chim. Acta 123 (1982) 221–231. [DOI] [PMID: 7116644]
2.  Jackson, M.C., Kucera, C.M. and Lenney, J.F. Purification and properties of human serum carnosinase. Clin. Chim. Acta 196 (1991) 193–206. [DOI] [PMID: 1903095]
[EC 3.4.13.20 created 1992]
 
 
EC 3.4.13.21     
Accepted name: dipeptidase E
Reaction: Dipeptidase E catalyses the hydrolysis of dipeptides Asp┼Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides
Other name(s): aspartyl dipeptidase; peptidase E; PepE gene product (Salmonella typhimurium)
Comments: A free carboxy group is not absolutely required in the substrate since Asp-Phe-NH2 and Asp-Phe-OMe are hydrolysed somewhat more slowly than dipeptides with free C-termini. No peptide larger than a C-blocked dipeptide is known to be a substrate. Asp-NH-Np is hydrolysed and is a convenient substrate for routine assay. The enzyme is most active near pH 7.0, and is not inhibited by di-isopropylfluorophosphate or phenylmethanesulfonyl fluoride. Belongs in peptidase family S51.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB
References:
1.  Haakansson, K., Wang, A.H.J. and Miller, C.G. The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad. Proc. Natl. Acad. Sci. USA 97 (2000) 14097–14102. [DOI] [PMID: 11106384]
2.  Lassy, R.A.L. and Miller, C.G. Peptidase E, a peptidase specific for N-terminal aspartic dipeptides, is a serine hydrolase. J. Bacteriol. 182 (2000) 2536–2543. [DOI] [PMID: 10762256]
[EC 3.4.13.21 created 2001]
 
 
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]
 
 


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