The Enzyme Database

Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB)

Proposed Changes to the Enzyme List

The entries below are proposed additions and amendments to the Enzyme Nomenclature list. They were prepared for the NC-IUBMB by Kristian Axelsen, Richard Cammack, Ron Caspi, Masaaki Kotera, Andrew McDonald, Gerry Moss, Dietmar Schomburg, Ida Schomburg and Keith Tipton. Comments and suggestions on these draft entries should be sent to Dr Andrew McDonald (Department of Biochemistry, Trinity College Dublin, Dublin 2, Ireland). The date on which an enzyme will be made official is appended after the EC number. To prevent confusion please do not quote new EC numbers until they are incorporated into the main list.

An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry.


Contents

*EC 1.1.1.206 tropinone reductase I
*EC 1.1.1.236 tropinone reductase II
*EC 1.2.1.19 aminobutyraldehyde dehydrogenase
EC 1.5.1.35 deleted
EC 1.14.13.102 psoralen synthase
EC 1.14.13.103 8-dimethylallylnaringenin 2′-hydroxylase
EC 2.5.1.70 naringenin 8-dimethylallyltransferase
EC 2.5.1.71 leachianone-G 2′′-dimethylallyltransferase
EC 2.6.1.84 arginine—pyruvate transaminase
EC 2.7.1.155 transferred
EC 2.7.4.24 diphosphoinositol-pentakisphosphate kinase
EC 3.2.1.163 1,6-α-D-mannosidase
EC 3.4.22.65 peptidase 1 (mite)
*EC 4.1.2.37 hydroxynitrilase
EC 4.1.2.39 deleted


*EC 1.1.1.206
Accepted name: tropinone reductase I
Reaction: tropine + NADP+ = tropinone + NADPH + H+
For diagram of reaction, click here
Glossary: tropine = 3α-hydroxytropane = tropan-3-endo-ol
Other name(s): tropine dehydrogenase; tropinone reductase (ambiguous); TR-I
Systematic name: tropine:NADP+ 3α-oxidoreductase
Comments: Also oxidizes other tropan-3α-ols, but not the corresponding β-derivatives [1]. This enzyme along with EC 1.1.1.236, tropinone reductase II, represents a branch point in tropane alkaloid metabolism [4]. Tropine (the product of EC 1.1.1.206) is incorporated into hyoscyamine and scopolamine whereas pseudotropine (the product of EC 1.1.1.236) is the first specific metabolite on the pathway to the calystegines [4]. Both enzymes are always found together in any given tropane-alkaloid-producing species, have a common substrate, tropinone, and are strictly stereospecific [3].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 118390-87-7
References:
1.  Koelen, K.J. and Gross, G.G. Partial purification and properties of tropine dehydrogenase from root cultures of Datura stramonium. Planta Med. 44 (1982) 227–230.
2.  Couladis, M.M, Friesen, J.B., Landgrebe, M.E. and Leete, E. Enzymes catalysing the reduction of tropinone to tropine and ψ-tropine isolated from the roots of Datura innoxia. Pytochemistry 30 (1991) 801–805.
3.  Nakajima, K., Hashimoto, T. and Yamada, Y. Two tropinone reductases with different stereospecificities are short-chain dehydrogenases evolved from a common ancestor. Proc. Natl. Acad. Sci. USA 90 (1993) 9591–9595. [PMID: 8415746]
4.  Dräger, B. Tropinone reductases, enzymes at the branch point of tropane alkaloid metabolism. Phytochemistry 67 (2006) 327–337. [PMID: 16426652]
[EC 1.1.1.206 created 1984, modified 2007]
 
 
*EC 1.1.1.236
Accepted name: tropinone reductase II
Reaction: pseudotropine + NADP+ = tropinone + NADPH + H+
For diagram of reaction, click here
Glossary: pseudotropine = ψ-tropine = 3β-hydroxytropane = tropan-3-exo-ol
Other name(s): tropinone (ψ-tropine-forming) reductase; pseudotropine forming tropinone reductase; tropinone reductase (ambiguous); TR-II
Systematic name: pseudotropine:NADP+ 3-oxidoreductase
Comments: This enzyme along with EC 1.1.1.206, tropine dehydrogenase, represents a branch point in tropane alkaloid metabolism [3]. Tropine (the product of EC 1.1.1.206) is incorporated into hyoscyamine and scopolamine whereas pseudotropine (the product of EC 1.1.1.236) is the first specific metabolite on the pathway to the calystegines [3]. Both enzymes are always found together in any given tropane-alkaloid-producing species, have a common substrate, tropinone, and are strictly stereospecific [2].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 136111-61-0
References:
1.  Dräger, B., Hashimoto, T. and Yamada, Y. Purification and characterization of pseudotropine forming tropinone reductase from Hyoscyamus niger root cultures. Agric. Biol. Chem. 52 (1988) 2663–2667.
2.  Couladis, M.M, Friesen, J.B., Landgrebe, M.E. and Leete, E. Enzymes catalysing the reduction of tropinone to tropine and ψ-tropine isolated from the roots of Datura innoxia. Pytochemistry 30 (1991) 801–805.
3.  Nakajima, K., Hashimoto, T. and Yamada, Y. Two tropinone reductases with different stereospecificities are short-chain dehydrogenases evolved from a common ancestor. Proc. Natl. Acad. Sci. USA 90 (1993) 9591–9595. [PMID: 8415746]
4.  Dräger, B. Tropinone reductases, enzymes at the branch point of tropane alkaloid metabolism. Phytochemistry 67 (2006) 327–337. [PMID: 16426652]
[EC 1.1.1.236 created 1992, modified 2007]
 
 
*EC 1.2.1.19
Accepted name: aminobutyraldehyde dehydrogenase
Reaction: 4-aminobutanal + NAD+ + H2O = 4-aminobutanoate + NADH + 2 H+
For diagram of arginine catabolism, click here
Glossary: 4-aminobutanoate = γ-aminobutyrate = GABA
Other name(s): γ-guanidinobutyraldehyde dehydrogenase (ambiguous); ABAL dehydrogenase; 4-aminobutyraldehyde dehydrogenase; 4-aminobutanal dehydrogenase; γ-aminobutyraldehyde dehydroganase; 1-pyrroline dehydrogenase; ABALDH; YdcW
Systematic name: 4-aminobutanal:NAD+ 1-oxidoreductase
Comments: The enzyme from some species exhibits broad substrate specificity and has a marked preference for straight-chain aldehydes (up to 7 carbon atoms) as substrates [9]. The plant enzyme also acts on 4-guanidinobutanal (cf. EC 1.2.1.54 γ-guanidinobutyraldehyde dehydrogenase). As 1-pyrroline and 4-aminobutanal are in equilibrium and can be interconverted spontaneously, 1-pyrroline may act as the starting substrate. The enzyme forms part of the arginine-catabolism pathway [8] and belongs in the aldehyde dehydrogenase superfamily [9].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 9028-98-2
References:
1.  Callewaert, D.M., Rosemblatt, M.S. and Tchen, T.T. Purification and properties of 4-aminobutanal dehydrogenase from a Pseudomonas species. J. Biol. Chem. 249 (1974) 1737–1741. [PMID: 4817964]
2.  Jakoby, W.B. Aldehyde dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 203–221.
3.  Jakoby, W.B. and Fredericks, J. Pyrrolidine and putrescine metabolism: γ-aminobutyraldehyde dehydrogenase. J. Biol. Chem. 234 (1959) 2145–2150. [PMID: 13673029]
4.  Matsuda, H. and Suzuki, Y. γ-Guanidinobutyraldehyde dehydrogenase of Vicia faba leaves. Plant Physiol. 76 (1984) 654–657. [PMID: 16663901]
5.  Yorifuji, T., Koike, K., Sakurai, T. and Yokoyama, K. 4-Aminobutyraldehyde and 4-guanidinobutyraldehyde dehydrogenases for arginine degradation in Pseudomonas putida. Agric. Biol. Chem. 50 (1986) 2009–2016.
6.  Prieto-Santos, M.I., Martin-Checa, J., Balaña-Fouce, R. and Garrido-Pertierra, A. A pathway for putrescine catabolism in Escherichia coli. Biochim. Biophys. Acta 880 (1986) 242–244. [PMID: 3510672]
7.  Prieto, M.I., Martin, J., Balaña-Fouce, R. and Garrido-Pertierra, A. Properties of γ-aminobutyraldehyde dehydrogenase from Escherichia coli. Biochimie 69 (1987) 1161–1168. [PMID: 3129020]
8.  Samsonova, N.N., Smirnov, S.V., Novikova, A.E. and Ptitsyn, L.R. Identification of Escherichia coli K12 YdcW protein as a γ-aminobutyraldehyde dehydrogenase. FEBS Lett. 579 (2005) 4107–4112. [PMID: 16023116]
9.  Gruez, A., Roig-Zamboni, V., Grisel, S., Salomoni, A., Valencia, C., Campanacci, V., Tegoni, M. and Cambillau, C. Crystal structure and kinetics identify Escherichia coli YdcW gene product as a medium-chain aldehyde dehydrogenase. J. Mol. Biol. 343 (2004) 29–41. [PMID: 15381418]
[EC 1.2.1.19 created 1965, modified 1989 (EC 1.5.1.35 created 2006, incorporated 2007)]
 
 
EC 1.5.1.35
Deleted entry: 1-pyrroline dehydrogenase. The enzyme is identical to EC 1.2.1.19, aminobutyraldehyde dehydrogenase, as the substrates 1-pyrroline and 4-aminobutanal are interconvertible
[EC 1.5.1.35 created 2006, deleted 2007]
 
 
EC 1.14.13.102
Accepted name: psoralen synthase
Reaction: (+)-marmesin + NADPH + H+ + O2 = psoralen + NADP+ + acetone + 2 H2O
For diagram of reaction, click here
Glossary: (+)-marmesin = (S)-2-(2-hydroxypropan-2-yl)-2,3-dihydro-7H-furo[3,2-g]chromen-7-one
psoralen = 7H-furo[3,2-g]chromen-7-one
Other name(s): CYP71AJ1
Systematic name: (+)-marmesin,NADPH:oxygen oxidoreductase
Comments: This microsomal cytochrome P-450-dependent enzyme is specific for (+)-marmesin, and to a much lesser extent 5-hydroxymarmesin, as substrate. Furanocoumarins protect plants from fungal invasion and herbivore attack. (+)-Columbianetin, the angular furanocoumarin analogue of the linear furanocoumarin (+)-marmesin, is not a substrate for the enzyme but it is a competitive inhibitor.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Larbat, R., Kellner, S., Specker, S., Hehn, A., Gontier, E., Hans, J., Bourgaud, F. and Matern, U. Molecular cloning and functional characterization of psoralen synthase, the first committed monooxygenase of furanocoumarin biosynthesis. J. Biol. Chem. 282 (2007) 542–554. [PMID: 17068340]
[EC 1.14.13.102 created 2007]
 
 
EC 1.14.13.103
Accepted name: 8-dimethylallylnaringenin 2′-hydroxylase
Reaction: sophoraflavanone B + NADPH + H+ + O2 = leachianone G + NADP+ + H2O
For diagram of sophoraflavanone G biosynthesis, click here
Glossary: sophoraflavanone B = (–)-(2S)-8-dimethylallylnaringenin = (–)-(2S)-5,7-dihydroxy-2-(4-hydroxyphenyl)-8-(3-methylbut-2-enyl)chroman-4-one
leachianone G = (–)-(2S)-2′-hydroxy-8-dimethylallylnaringenin = (–)-(2S)-5,7-dihydroxy-8-(2-hydroxy-3-methylbut-2-enyl)-2-(4-hydroxyphenyl)chroman-4-one
Other name(s): 8-DMAN 2′-hydroxylase
Systematic name: sophoraflavanone-B,NADPH:oxygen oxidoreductase (2′-hydroxylating)
Comments: A membrane-bound cytochrome P-450 heme-thiolate monooxygenase that is associated with the endoplasmic reticulum [1,2]. This enzyme is specific for sophoraflavanone B as substrate. NADPH cannot be replaced by NADH, FAD or FMN. Along with EC 2.5.1.70 (naringenin 8-dimethylallyltransferase) and EC 2.5.1.71 (leachianone G 2′′-dimethylallyltransferase), this enzyme forms part of the sophoraflavanone-G-biosynthesis pathway.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Yamamoto, H., Yatou, A. and Inoue, K. 8-Dimethylallylnaringenin 2′-hydroxylase, the crucial cytochrome P450 mono-oxygenase for lavandulylated flavanone formation in Sophora flavescens cultured cells. Phytochemistry 58 (2001) 671–676. [PMID: 11672730]
2.  Zhao, P., Inoue, K., Kouno, I. and Yamamoto, H. Characterization of leachianone G 2′′-dimethylallyltransferase, a novel prenyl side-chain elongation enzyme for the formation of the lavandulyl group of sophoraflavanone G in Sophora flavescens Ait. cell suspension cultures. Plant Physiol. 133 (2003) 1306–1313. [PMID: 14551337]
[EC 1.14.13.103 created 2007]
 
 
EC 2.5.1.70
Accepted name: naringenin 8-dimethylallyltransferase
Reaction: dimethylallyl diphosphate + (-)-(2S)-naringenin = diphosphate + sophoraflavanone B
For diagram of sophoraflavanone-G biosynthesis, click here
Glossary: (-)-(2S)-naringenin = (-)-(2S)-5,7-dihydroxy-2-(4-hydroxyphenyl)chroman-4-one
sophoraflavanone B = (-)-(2S)-8-dimethylallylnaringenin = (-)-(2S)-5,7-dihydroxy-2-(4-hydroxyphenyl)-8-(3-methylbut-2-enyl)chroman-4-one
Other name(s): N8DT
Systematic name: dimethylallyl-diphosphate:naringenin 8-dimethylallyltransferase
Comments: Requires Mg2+. This membrane-bound protein is located in the plastids [2]. In addition to naringenin, the enzyme can prenylate several other flavanones at the C-8 position, but more slowly. Along with EC 1.14.13.103 (8-dimethylallylnaringenin 2′-hydroxylase) and EC 2.5.1.71 (leachianone G 2′′-dimethylallyltransferase), this enzyme forms part of the sophoraflavanone-G-biosynthesis pathway.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Yamamoto, H., Senda, M. and Inoue, K. Flavanone 8-dimethylallyltransferase in Sophora flavescens cell suspension cultures. Phytochemistry 54 (2000) 649–655. [PMID: 10975499]
2.  Zhao, P., Inoue, K., Kouno, I. and Yamamoto, H. Characterization of leachianone G 2′′-dimethylallyltransferase, a novel prenyl side-chain elongation enzyme for the formation of the lavandulyl group of sophoraflavanone G in Sophora flavescens Ait. cell suspension cultures. Plant Physiol. 133 (2003) 1306–1313. [PMID: 14551337]
[EC 2.5.1.70 created 2007]
 
 
EC 2.5.1.71
Accepted name: leachianone-G 2′′-dimethylallyltransferase
Reaction: dimethylallyl diphosphate + leachianone G = diphosphate + sophoraflavanone G
For diagram of sophoraflavanone-G biosynthesis, click here
Glossary: leachianone G = (-)-(2S)-2′-hydroxy-8-dimethylallylnaringenin = (-)-(2S)-5,7-dihydroxy-8-(2-hydroxy-3-methylbut-2-enyl)-2-(4-hydroxyphenyl)chroman-4-one
sophoraflavanone G = 2-{[(2S)-2-(2,4-dihydroxyphenyl)-5,7-dihydroxy-4-oxo-chroman-8-yl]methyl}-5-methyl-hex-4-enoic acid
Other name(s): LG 2′′-dimethylallyltransferase; leachianone G 2′′-dimethylallyltransferase; LGDT
Systematic name: dimethylallyl-diphosphate:leachianone-G 2′′-dimethylallyltransferase
Comments: This membrane-bound enzyme is located in the plastids and requires Mg2+ for activity. The reaction forms the lavandulyl sidechain of sophoraflavanone G by transferring a dimethylallyl group to the 2′′ position of another dimethylallyl group attached at postiion 8 of leachianone G. The enzyme is specific for dimethylallyl diphosphate as the prenyl donor, as it cannot be replaced by isopentenyl diphosphate or geranyl diphosphate. Euchrenone a7 (a 5-deoxy derivative of leachianone G) and kenusanone I (a 7-methoxy derivative of leachianone G) can also act as substrates, but more slowly. Along with EC 1.14.13.103 (8-dimethylallylnaringenin 2′-hydroxylase) and EC 2.5.1.70 (naringenin 8-dimethylallyltransferase), this enzyme forms part of the sophoraflavanone-G-biosynthesis pathway.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Zhao, P., Inoue, K., Kouno, I. and Yamamoto, H. Characterization of leachianone G 2′′-dimethylallyltransferase, a novel prenyl side-chain elongation enzyme for the formation of the lavandulyl group of sophoraflavanone G in Sophora flavescens Ait. cell suspension cultures. Plant Physiol. 133 (2003) 1306–1313. [PMID: 14551337]
[EC 2.5.1.71 created 2007]
 
 
EC 2.6.1.84
Accepted name: arginine—pyruvate transaminase
Reaction: L-arginine + pyruvate = 5-guanidino-2-oxopentanoate + L-alanine
For diagram of arginine-catabolism pathway, click here
Other name(s): arginine:pyruvate transaminase; AruH; ATase
Systematic name: L-arginine:pyruvate aminotransferase
Comments: A pyridoxal-phosphate protein. While L-arginine is the best substrate, the enzyme exhibits broad substrate specificity, with L-lysine, L-methionine, L-leucine, L-ornithine and L-glutamine also able to act as substrates, but more slowly. Pyruvate cannot be replaced by 2-oxoglutarate as amino-group acceptor. This is the first catalytic enzyme of the arginine transaminase pathway for L-arginine utilization in Pseudomonas aeruginosa. This pathway is only used when the major route of arginine catabolism, i.e. the arginine succinyltransferase pathway, is blocked.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Yang, Z. and Lu, C.-D. Characterization of an arginine:pyruvate transaminase in arginine catabolism of Pseudomonas aeruginosa PAO1. J. Bacteriol. 189 (2007) 3954–3959. [PMID: 17416668]
2.  Yang, Z. and Lu, C.D. Functional genomics enables identification of genes of the arginine transaminase pathway in Pseudomonas aeruginosa. J. Bacteriol. 189 (2007) 3945–3953. [PMID: 17416670]
[EC 2.6.1.84 created 2007]
 
 
EC 2.7.1.155
Transferred entry: diphosphoinositol-pentakisphosphate kinase. Now EC 2.7.4.24, diphosphoinositol-pentakisphosphate kinase. The enzyme had been incorrectly classified as the reaction involves transfer of a phospho group to another phospho group (EC 2.7.4) rather than to an hydroxy group (EC 2.7.1)
[EC 2.7.1.155 created 2003, deleted 2007]
 
 
EC 2.7.4.24
Accepted name: diphosphoinositol-pentakisphosphate kinase
Reaction: (1) ATP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
(2) ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
Other name(s): PP-IP5 kinase; diphosphoinositol pentakisphosphate kinase; ATP:5-diphospho-1D-myo-inositol-pentakisphosphate phosphotransferase; PP-InsP5 kinase; PPIP5K; PPIP5K1; PPIP5K2; VIP1; VIP2
Systematic name: ATP:1D-myo-inositol-5-diphosphate-pentakisphosphate phosphotransferase
Comments: This enzyme is activated by osmotic shock [4]. Ins(1,3,4,5,6)P5, 1D-myo-inositol diphosphate tetrakisphosphate and 1D-myo-inositol bisdiphosphate triphosphate are not substrates [4].
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG
References:
1.  Shears, S.B., Ali, N., Craxton, A. and Bembenek, M.E. Synthesis and metabolism of bis-diphosphoinositol tetrakisphosphate in vitro and in vivo. J. Biol. Chem. 270 (1995) 10489–10497. [PMID: 7737983]
2.  Albert, C., Safrany, S.T., Bembenek, M.E., Reddy, K.M., Reddy, K.K., Falck, J.-R., Bröcker, M., Shears, S.B. and Mayr, G.W. Biological variability in the structures of diphosphoinositol polyphosphates in Dictyostelium discoideum and mammalian cells. Biochem. J. 327 (1997) 553–560. [PMID: 9359429]
3.  Fridy, P.C., Otto, J.C., Dollins, D.E. and York, J.D. Cloning and characterization of two human VIP1-like inositol hexakisphosphate and diphosphoinositol pentakisphosphate kinases. J. Biol. Chem. 282 (2007) 30754–30762. [PMID: 17690096]
4.  Choi, J.H., Williams, J., Cho, J., Falck, J.R. and Shears, S.B. Purification, sequencing, and molecular identification of a mammalian PP-InsP5 kinase that Is activated when cells are exposed to hyperosmotic stress. J. Biol. Chem. 282 (2007) 30763–30775. [PMID: 17702752]
5.  Lin, H., Fridy, P.C., Ribeiro, A.A., Choi, J.H., Barma, D.K., Vogel, G., Falck, J.R., Shears, S.B., York, J.D. and Mayr, G.W. Structural analysis and detection of biological inositol pyrophosphates reveal that the family of VIP/diphosphoinositol pentakisphosphate kinases are 1/3-kinases. J. Biol. Chem. 284 (2009) 1863–1872. [PMID: 18981179]
6.  Wang, H., Falck, J.R., Hall, T.M. and Shears, S.B. Structural basis for an inositol pyrophosphate kinase surmounting phosphate crowding. Nat. Chem. Biol. 8 (2012) 111–116. [PMID: 22119861]
[EC 2.7.4.24 created 2003 as EC 2.7.1.155, transferred 2007 to EC 2.7.4.24, modified 2014]
 
 
EC 3.2.1.163
Accepted name: 1,6-α-D-mannosidase
Reaction: Hydrolysis of the (1→6)-linked α-D-mannose residues in α-D-Manp-(1→6)-D-Manp
Systematic name: (1→6)-α-mannosyl α-D-mannohydrolase
Comments: The enzyme is specific for (1→6)-linked mannobiose and has no activity towards any other linkages, or towards p-nitrophenyl-α-D-mannopyranoside or baker’s yeast mannan. It is strongly inhibited by Mn2+ but does not require Ca2+ or any other metal cofactor for activity.
Links to other databases: BRENDA, EXPASY, IUBMB
References:
1.  Athanasopoulos, V.I., Niranjan, K. and Rastall, R.A. The production, purification and characterisation of two novel α-D-mannosidases from Aspergillus phoenicis. Carbohydr. Res. 340 (2005) 609–617. [PMID: 15721331]
[EC 3.2.1.163 created 2007]
 
 
EC 3.4.22.65
Accepted name: peptidase 1 (mite)
Reaction: Broad endopeptidase specificity
Other name(s): allergen Der f 1; allergen Der p 1; antigen Der p 1; antigen Eur m 1; antigen Pso o 1; major mite fecal allergen Der p 1; Der p 1; Der f 1; Eur m 1; endopeptidase 1 (mite)
Comments: This enzyme, derived from the house dust mite, is a major component of the allergic immune response [2]. The substrate specificity of this enzyme is not altogether clear. It cleaves the low-affinity IgE receptor CD23 at Glu298┼Ser299 and Ser155┼Ser156 [1]. It also cleaves the pulmonary structural proteins occludin and claudin at Leu┼Leu, Asp┼Leu and at Gly┼Thr bonds [1,2]. It can also cleave the α subunit of the interleukin-2 (IL-2) receptor (CD25) [4]. Using a positional scanning combinatorial library, it was found that the major substrate-specificity determinant is for Ala in the P2 position [3]. The enzyme shows only a slight preference for basic amino acids in the P1 and P3 positions and a preference for aliphatic amino acids such as Ile, Pro, Val, Leu and norleucine in the P4 position [3]. Belongs in peptidase family C1A.
Links to other databases: BRENDA, EXPASY, IUBMB, KEGG, PDB
References:
1.  Meighan, P. and Pirzad, R. Mite endopeptidase 1. In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds), Handbook of Proteolytic Enzymes, 2nd edn, Elsevier, London, 2004, pp. 1187–1189.
2.  Kalsheker, N.A., Deam, S., Chambers, L., Sreedharan, S., Brocklehurst, K. and Lomas, D.A. The house dust mite allergen Der p1 catalytically inactivates α1-antitrypsin by specific reactive centre loop cleavage: a mechanism that promotes airway inflammation and asthma. Biochem. Biophys. Res. Commun. 221 (1996) 59–61. [PMID: 8660343]
3.  Harris, J., Mason, D.E., Li, J., Burdick, K.W., Backes, B.J., Chen, T., Shipway, A., Van Heeke, G., Gough, L., Ghaemmaghami, A., Shakib, F., Debaene, F. and Winssinger, N. Activity profile of dust mite allergen extract using substrate libraries and functional proteomic microarrays. Chem. Biol. 11 (2004) 1361–1372. [PMID: 15489163]
4.  Schulz, O., Sewell, H.F. and Shakib, F. Proteolytic cleavage of CD25, the α subunit of the human T cell interleukin 2 receptor, by Der p 1, a major mite allergen with cysteine protease activity. J. Exp. Med. 187 (1998) 271–275. [PMID: 9432986]
5.  Schulz, O., Sewell, H.F. and Shakib, F. A sensitive fluorescent assay for measuring the cysteine protease activity of Der p 1, a major allergen from the dust mite Dermatophagoides pteronyssinus. Mol. Pathol. 51 (1998) 222–224. [PMID: 9893750]
6.  Takai, T., Kato, T., Sakata, Y., Yasueda, H., Izuhara, K., Okumura, K. and Ogawa, H. Recombinant Der p 1 and Der f 1 exhibit cysteine protease activity but no serine protease activity. Biochem. Biophys. Res. Commun. 328 (2005) 944–952. [PMID: 15707969]
[EC 3.4.22.65 created 2007]
 
 
*EC 4.1.2.37
Deleted entry: hydroxynitrilase. Now covered by EC 4.1.2.46 [aliphatic (R)-hydroxynitrile lyase] and EC 4.1.2.47 [(S)-hydroxynitrile ketone-lyase (cyanide forming)]
[EC 4.1.2.37 created 1992 (EC 4.1.2.39 created 1999, incorporated 2007), deleted 2011]
 
 
EC 4.1.2.39
Deleted entry: hydroxynitrilase. The enzyme is identical to EC 4.1.2.37, hydroxynitrilase
[EC 4.1.2.39 created 1999, deleted 2007]
 
 


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