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 Keith Tipton, Sinéad Boyce, Gerry Moss and Hal Dixon, with occasional help from other Committee members. Comments and suggestions on these draft entries should be sent to Professor K.F. Tipton and Dr S. Boyce (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To prevent confusion, please do not quote new EC numbers until they are incorporated into the main list.

Many thanks to those of you who have submitted details of new enzymes or updates to existing enzymes.

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

Contents

EC 1.2.1.73 sulfoacetaldehyde dehydrogenase
EC 1.3.1.81 (+)-pulegone reductase
*EC 1.4.3.4 monoamine oxidase
EC 1.4.3.6 deleted
EC 1.4.3.21 primary-amine oxidase
EC 1.4.3.22 diamine oxidase
EC 1.14.13.104 (+)-menthofuran synthase
EC 1.14.19.4 Δ8-fatty-acid desaturase
EC 2.4.1.245 α,α-trehalose synthase
EC 3.1.26.12 ribonuclease E
EC 3.4.11.24 aminopeptidase S

EC 1.2.1.73 – public review until 29 August 2008 [Last modified: 2008-08-01 11:55:25]
Accepted name: sulfoacetaldehyde dehydrogenase
Reaction: 2-sulfoacetaldehyde + H2O + NAD+ = sulfoacetate + NADH + 2 H+
Glossary: 2-sulfoacetaldehyde = 2-oxoethanesulfonate
taurine = 2-aminoethanesulfonate
Other name(s): SafD
Systematic name: 2-sulfoacetaldehyde:NAD+ oxidoreductase
Comments: This reaction is part of a bacterial pathway that can utilize the amino group of taurine as a sole source of nitrogen for growth. At physiological concentrations, NAD+ cannot be replaced by NADP+. The enzyme is specific for sulfoacetaldehyde, as formaldehyde, acetaldehyde, betaine aldehyde, propanal, glyceraldehyde, phosphonoaldehyde, glyoxylate, glycolaldehyde and 2-oxobutyrate are not substrates.
References:
1.  Krejčík, Z., Denger, K., Weinitschke, S., Hollemeyer, K., Pačes, V., Cook, A.M. and Smits, T.H.M. Sulfoacetate released during the assimilation of taurine-nitrogen by Neptuniibacter caesariensis: purification of sulfoacetaldehyde dehydrogenase. Arch. Microbiol. 190 (2008) 159–168. [PMID: 18506422]
[EC 1.2.1.73 created 2008]
 
 
EC 1.3.1.81 – public review until 29 August 2008 [Last modified: 2008-08-01 11:59:47]
Accepted name: (+)-pulegone reductase
Reaction: (1) (-)-menthone + NADP+ = (+)-pulegone + NADPH + H+
(2) (+)-isomenthone + NADP+ = (+)-pulegone + NADPH + H+
Systematic name: (-)-menthone:NADP+ oxidoreductase
Comments: NADH cannot replace NADPH as reductant. The Δ8,9-double bond of (+)-cis-isopulegone and the Δ1,2-double bond of (±)-piperitone are not substrates. The enzyme from peppermint (Mentha x piperita) converts (+)-pulegone into both (-)-menthone and (+)-isomenthone at a ratio of 70:30 for native enzyme but it does not catalyse the reverse reaction. This enzyme is a member of the medium-chain dehydrogenase/reductase superfamily.
References:
1.  Ringer, K.L., McConkey, M.E., Davis, E.M., Rushing, G.W. and Croteau, R. Monoterpene double-bond reductases of the (-)-menthol biosynthetic pathway: isolation and characterization of cDNAs encoding (-)-isopiperitenone reductase and (+)-pulegone reductase of peppermint. Arch. Biochem. Biophys. 418 (2003) 80–92. [PMID: 13679086]
[EC 1.3.1.81 created 2008]
 
 
*EC 1.4.3.4 – public review until 29 August 2008 [Last modified: 2008-08-01 12:02:47]
Accepted name: monoamine oxidase
Reaction: RCH2NHR′ + H2O + O2 = RCHO + R′NH2 + H2O2
Other name(s): adrenalin oxidase; adrenaline oxidase; amine oxidase (ambiguous); amine oxidase (flavin-containing); amine:oxygen oxidoreductase (deaminating) (flavin-containing); epinephrine oxidase; MAO; MAO A; MAO B; MAO-A; MAO-B; monoamine oxidase A; monoamine oxidase B; monoamine:O2 oxidoreductase (deaminating); polyamine oxidase (ambiguous); serotonin deaminase; spermidine oxidase (ambiguous); spermine oxidase (ambiguous); tyraminase; tyramine oxidase
Systematic name: amine:oxygen oxidoreductase (deaminating)
Comments: A mitochondrial outer-membrane flavoprotein (FAD) that catalyses the oxidative deamination of neurotransmitters and biogenic amines [3]. Acts on primary amines, and also on some secondary and tertiary amines. It differs from EC 1.4.3.21, primary-amine oxidase as it can oxidize secondary and tertiary amines but not methylamine. This enzyme is inhibited by acetylenic compounds such as chlorgyline, 1-deprenyl and pargyline but, unlike EC 1.4.3.21 and EC 1.4.3.22 (diamine oxidase), it is not inhibited by semicarbazide.
Links to other databases: BRENDA, ERGO, EXPASY, IUBMB, KEGG, PDB, CAS registry number: 9001-66-5
References:
1.  Blaschko, H. Amine oxidase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, vol. 8, Academic Press, New York, 1963, pp. 337–351.
2.  Dostert, P.L., Strolin Benedetti, M. and Tipton, K.F. Interactions of monoamine oxidase with substrates and inhibitors. Med. Res. Rev. 9 (1989) 45–89. [PMID: 2644497]
3.  Edmondson, D.E., Mattevi, A., Binda, C., Li, M. and Hubálek, F. Structure and mechanism of monoamine oxidase. Curr. Med. Chem. 11 (2004) 1983–1993. [PMID: 15279562]
4.  Shih, J.C. and Chen, K. Regulation of MAO-A and MAO-B gene expression. Curr. Med. Chem. 11 (2004) 1995–2005. [PMID: 15279563]
5.  Tipton, K.F., Boyce, S., O'Sullivan, J., Davey, G.P. and Healy, J. Monoamine oxidases: certainties and uncertainties. Curr. Med. Chem. 11 (2004) 1965–1982. [PMID: 15279561]
6.  De Colibus, L., Li, M., Binda, C., Lustig, A., Edmondson, D.E. and Mattevi, A. Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B. Proc. Natl. Acad. Sci. USA 102 (2005) 12684–12689. [PMID: 16129825]
7.  Youdim, M.B., Edmondson, D. and Tipton, K.F. The therapeutic potential of monoamine oxidase inhibitors. Nat. Rev. Neurosci. 7 (2006) 295–309. [PMID: 16552415]
8.  Youdim, M.B. and Bakhle, Y.S. Monoamine oxidase: isoforms and inhibitors in Parkinson′s disease and depressive illness. Br. J. Pharmacol. 147 Suppl. 1 (2006) S287–S296. [PMID: 16402116]
[EC 1.4.3.4 created 1961, modified 1983 (EC 1.4.3.9 created 1972, incorporated 1984), modified 2008]
 
 
EC 1.4.3.6 – public review until 29 August 2008 [Last modified: 2008-08-01 12:03:05]
Deleted entry: amine oxidase (copper-containing). This was classified on the basis of cofactor content rather than reaction catalysed and is now known to contain two distinct enzyme activities. It has been replaced by two enzymes, EC 1.4.3.21 (primary-amine oxidase) and EC 1.4.3.22 (diamine oxidase)
[EC 1.4.3.6 created 1961, modified 1983, modified 1989, deleted 2008]
 
 
EC 1.4.3.21 – public review until 29 August 2008 [Last modified: 2008-08-01 12:04:35]
Accepted name: primary-amine oxidase
Reaction: RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2
Other name(s): amine oxidase (ambiguous); amine oxidase (copper-containing); amine oxidase (pyridoxal containing) (incorrect); benzylamine oxidase (incorrect); CAO (ambiguous); copper amine oxidase (ambiguous); Cu-amine oxidase (ambiguous); Cu-containing amine oxidase (ambiguous); diamine oxidase (incorrect); diamino oxhydrase (incorrect); histamine deaminase (ambiguous); histamine oxidase (ambiguous); monoamine oxidase (ambiguous); plasma monoamine oxidase (ambiguous); polyamine oxidase (ambiguous); semicarbazide-sensitive amine oxidase (ambiguous); SSAO (ambiguous)
Systematic name: primary-amine:oxygen oxidoreductase (deaminating)
Comments: A group of enzymes that oxidize primary monoamines but have little or no activity towards diamines, such as histamine, or towards secondary and tertiary amines. They are copper quinoproteins (2,4,5-trihydroxyphenylalanine quinone) and, unlike EC 1.4.3.4, monoamine oxidase, are sensitive to inhibition by carbonyl-group reagents, such as semicarbazide. In some mammalian tissues the enzyme also functions as a vascular-adhesion protein (VAP-1).
References:
1.  Haywood, G.W. and Large, P.J. Microbial oxidation of amines. Distribution, purification and properties of two primary-amine oxidases from the yeast Candida boidinii grown on amines as sole nitrogen source. Biochem. J. 199 (1981) 187–201. [PMID: 7337701]
2.  Tipping, A.J. and McPherson, M.J. Cloning and molecular analysis of the pea seedling copper amine oxidase. J. Biol. Chem. 270 (1995) 16939–16946. [PMID: 7622512]
3.  Lyles, G.A. Mammalian plasma and tissue-bound semicarbazide-sensitive amine oxidases: biochemical, pharmacological and toxicological aspects. Int. J. Biochem. Cell Biol. 28 (1996) 259–274. [PMID: 8920635]
4.  Wilce, M.C., Dooley, D.M., Freeman, H.C., Guss, J.M., Matsunami, H., McIntire, W.S., Ruggiero, C.E., Tanizawa, K. and Yamaguchi, H. Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone. Biochemistry 36 (1997) 16116–16133. [PMID: 9405045]
5.  Lee, Y. and Sayre, L.M. Reaffirmation that metabolism of polyamines by bovine plasma amine oxidase occurs strictly at the primary amino termini. J. Biol. Chem. 273 (1998) 19490–19494. [PMID: 9677370]
6.  Houen, G. Mammalian Cu-containing amine oxidases (CAOs): new methods of analysis, structural relationships, and possible functions. APMIS Suppl. 96 (1999) 1–46. [PMID: 10668504]
7.  Andrés, N., Lizcano, J.M., Rodríguez, M.J., Romera, M., Unzeta, M. and Mahy, N. Tissue activity and cellular localization of human semicarbazide-sensitive amine oxidase. J. Histochem. Cytochem. 49 (2001) 209–217. [PMID: 11156689]
8.  Saysell, C.G., Tambyrajah, W.S., Murray, J.M., Wilmot, C.M., Phillips, S.E., McPherson, M.J. and Knowles, P.F. Probing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue. Biochem. J. 365 (2002) 809–816. [PMID: 11985492]
9.  O'Sullivan, J., Unzeta, M., Healy, J., O'Sullivan, M.I., Davey, G. and Tipton, K.F. Semicarbazide-sensitive amine oxidases: enzymes with quite a lot to do. Neurotoxicology 25 (2004) 303–315. [PMID: 14697905]
10.  Airenne, T.T., Nymalm, Y., Kidron, H., Smith, D.J., Pihlavisto, M., Salmi, M., Jalkanen, S., Johnson, M.S. and Salminen, T.A. Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications. Protein Sci. 14 (2005) 1964–1974. [PMID: 16046623]
[EC 1.4.3.21 created 2007 (EC 1.4.3.6 created 1961, part-incorporated 2008)]
 
 
EC 1.4.3.22 – public review until 29 August 2008 [Last modified: 2008-08-01 12:05:52]
Accepted name: diamine oxidase
Reaction: histamine + H2O + O2 = (imidazol-4-yl)acetaldehyde + NH3 + H2O2
Other name(s): amine oxidase (ambiguous); amine oxidase (copper-containing) (ambiguous); CAO (ambiguous); Cu-containing amine oxidase (ambiguous); copper amine oxidase (ambiguous); diamine oxidase (ambiguous); diamino oxhydrase (ambiguous); histaminase; histamine deaminase (incorrect); semicarbazide-sensitive amine oxidase (incorrect); SSAO (incorrect)
Systematic name: histamine:oxygen oxidoreductase (deaminating)
Comments: A group of enzymes that oxidize diamines, such as histamine, and also some primary monoamines but have little or no activity towards secondary and tertiary amines. They are copper quinoproteins (2,4,5-trihydroxyphenylalanine quinone) and, like EC 1.4.3.21 (primary-amine oxidase) but unlike EC 1.4.3.4 (monoamine oxidase), they are sensitive to inhibition by carbonyl-group reagents, such as semicarbazide.
References:
1.  Zeller, E.A. Diamine oxidases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, vol. 8, Academic Press, New York, 1963, pp. 313–335.
2.  Crabbe, M.J., Waight, R.D., Bardsley, W.G., Barker, R.W., Kelly, I.D. and Knowles, P.F. Human placental diamine oxidase. Improved purification and characterization of a copper- and manganese-containing amine oxidase with novel substrate specificity. Biochem. J. 155 (1976) 679–687. [PMID: 182134]
3.  Chassande, O., Renard, S., Barbry, P. and Lazdunski, M. The human gene for diamine oxidase, an amiloride binding protein. Molecular cloning, sequencing, and characterization of the promoter. J. Biol. Chem. 269 (1994) 14484–14489. [PMID: 8182053]
4.  Houen, G. Mammalian Cu-containing amine oxidases (CAOs): new methods of analysis, structural relationships, and possible functions. APMIS Suppl. 96 (1999) 1–46. [PMID: 10668504]
5.  Elmore, B.O., Bollinger, J.A. and Dooley, D.M. Human kidney diamine oxidase: heterologous expression, purification, and characterization. J. Biol. Inorg. Chem. 7 (2002) 565–579. [PMID: 12072962]
[EC 1.4.3.22 created 2007 (EC 1.4.3.6 created 1961, part-incorporated 2008)]
 
 
EC 1.14.13.104 – public review period expired (19 August 2008) [Last modified: 2008-07-22 09:04:40]
Accepted name: (+)-menthofuran synthase
Reaction: (+)-pulegone + NADPH + H+ + O2 = (+)-menthofuran + NADP+ + H2O
For diagram of (-)-carvone, perillyl aldehyde and pulegone biosynthesis, click here and for mechanism of reaction, click here
Other name(s): menthofuran synthase; (+)-pulegone 9-hydroxylase; (+)-MFS; cytochrome P450 menthofuran synthase
Systematic name: (+)-pulegone,NADPH:oxygen oxidoreductase (9-hydroxylating)
Comments: A heme-thiolate protein (P-450). The conversion of substrate into product involves the hydroxylation of the syn-methyl (C9), intramolecular cyclization to the hemiketal and dehydration to the furan [1]. This is the second cytochrome P-450-mediated step of monoterpene metabolism in peppermint, with the other step being catalysed by EC 1.14.13.47, (S)-limonene 3-monooxygenase [1].
References:
1.  Bertea, C.M., Schalk, M., Karp, F., Maffei, M. and Croteau, R. Demonstration that menthofuran synthase of mint (Mentha) is a cytochrome P450 monooxygenase: cloning, functional expression, and characterization of the responsible gene. Arch. Biochem. Biophys. 390 (2001) 279–286. [PMID: 11396930]
2.  Mahmoud, S.S. and Croteau, R.B. Menthofuran regulates essential oil biosynthesis in peppermint by controlling a downstream monoterpene reductase. Proc. Natl. Acad. Sci. USA 100 (2003) 14481–14486. [PMID: 14623962]
[EC 1.14.13.104 created 2008]
 
 
EC 1.14.19.4 – public review until 29 August 2008 [Last modified: 2008-08-01 12:08:30]
Accepted name: Δ8-fatty-acid desaturase
Reaction: phytosphinganine + reduced acceptor + O2 = Δ8-phytosphingenine + acceptor + 2 H2O
Glossary: phytosphinganine = 4-hydroxysphinganine
Other name(s): Δ8-sphingolipid desaturase; EFD1; BoDES8; SLD; Δ8 fatty acid desaturase; Δ8-desaturase
Systematic name: phytosphinganine,hydrogen donor:oxygen Δ8-oxidoreductase
Comments: This enzyme, which has been found mainly in plants, introduces a double bond at Δ8 of C18 and C20 fatty acids [2]. The enzyme from the marine microalga Euglena gracilis requires a double bond to be present at Δ11 and is most active with 20:3 Δ11,14,17 and 20:2 Δ11,14 as substrates, although it can also desaturate 20:1 Δ11 [1]. The Δ8-desaturation pathway represents an alternate pathway for the synthesis of the polyunsaturated fatty acids arachidonate (C20:4 Δ5,14) and eicosapentaenoate (C20:5 Δ5,17) in organisms lacking a Δ6-desaturase [1]. The enzyme from the sunflower Helianthus annuus and from the herb Borago officinalis comprises a C-terminal desaturase domain and an N-terminal cytochrome-b5 domain [2].
References:
1.  Wallis, J.G. and Browse, J. The Δ8-desaturase of Euglena gracilis: an alternate pathway for synthesis of 20-carbon polyunsaturated fatty acids. Arch. Biochem. Biophys. 365 (1999) 307–316. [PMID: 10328826]
2.  Sperling, P., Libisch, B., Zähringer, U., Napier, J.A. and Heinz, E. Functional identification of a Δ8-sphingolipid desaturase from Borago officinalis. Arch. Biochem. Biophys. 388 (2001) 293–298. [PMID: 11368168]
3.  Takakuwa, N., Kinoshita, M., Oda, Y. and Ohnishi, M. Isolation and characterization of the genes encoding Δ8-sphingolipid desaturase from Saccharomyces kluyveri and Kluyveromyces lactis. Curr. Microbiol. 45 (2002) 459–461. [PMID: 12402089]
4.  Beckmann, C., Rattke, J., Oldham, N.J., Sperling, P., Heinz, E. and Boland, W. Characterization of a Δ8-sphingolipid desaturase from higher plants: a stereochemical and mechanistic study on the origin of E,Z isomers. Angew. Chem. Int. Ed. Engl. 41 (2002) 2298–2300. [PMID: 12203571]
[EC 1.14.19.4 created 2008]
 
 
EC 2.4.1.245 – public review until 29 August 2008 [Last modified: 2008-08-01 11:49:57]
Accepted name: α,α-trehalose synthase
Reaction: ADP-glucose + D-glucose = α,α-trehalose + ADP
Other name(s): trehalose synthase; trehalose synthetase; UDP-glucose:glucose 1-glucosyltransferase; TreT; PhGT
Systematic name: ADP-glucose:D-glucose 1-α-D-glucosyltransferase
Comments: Requires Mg2+ for maximal activity [1]. The enzyme-catalysed reaction is reversible [1]. In the reverse direction to that shown above, the enzyme is specific for α,α-trehalose as substrate, as it cannot use α- or β-paranitrophenyl glucosides, maltose, sucrose, lactose or cellobiose [1]. While the enzyme from the hyperthermophilic archaeon Pyrococcus horikoshii can use ADP-, UDP- and GDP-glucose to the same extent [2], that from Thermococcus litoralis has a marked preference for ADP [1].
References:
1.  Qu, Q., Lee, S.J. and Boos, W. TreT, a novel trehalose glycosyltransferring synthase of the hyperthermophilic archaeon Thermococcus litoralis. J. Biol. Chem. 279 (2004) 47890–47897. [PMID: 15364950]
2.  Ryu, S.I., Park, C.S., Cha, J., Woo, E.J. and Lee, S.B. A novel trehalose-synthesizing glycosyltransferase from Pyrococcus horikoshii: molecular cloning and characterization. Biochem. Biophys. Res. Commun. 329 (2005) 429–436. [PMID: 15737605]
[EC 2.4.1.245 created 2008]
 
 
EC 3.1.26.12 – public review until 29 August 2008 [Last modified: 2008-08-01 12:11:21]
Accepted name: ribonuclease E
Reaction: Endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions
Other name(s): endoribonuclease E; RNase E; Rne protein
Comments: RNase E is a bacterial ribonuclease that plays a role in the processing of ribosomal RNA (9S to 5S rRNA), the chemical degradation of bulk cellular RNA, the decay of specific regulatory, messenger and structural RNAs and the control of plasmid DNA replication [1]. The enzyme binds to monophosphorylated 5′ ends of substrates but exhibits sequential cleavages in the 3′ to 5′ direction [1]. 2′-O-Methyl nucleotide substitutions at RNase E binding sites do not prevent binding but do prevent cleavage of non-modified target sequences 5′ to that locus [1]. In Escherichia coli, the enzyme is found in the RNA degradosome. The C-terminal half of the protein contains binding sites for the three other major degradosomal components, the DEAD-box RNA helicase Rh1B, enolase (EC 4.1.1.11) and polynucleotide phosphorylase (EC 2.7.7.8).
References:
1.  Feng, Y., Vickers, T.A. and Cohen, S.N. The catalytic domain of RNase E shows inherent 3′ to 5′ directionality in cleavage site selection. Proc. Natl. Acad. Sci. USA 99 (2002) 14746–14751. [PMID: 12417756]
2.  Ehretsmann, C.P., Carpousis, A.J. and Krisch, H.M. Specificity of Escherichia coli endoribonuclease RNase E: in vivo and in vitro analysis of mutants in a bacteriophage T4 mRNA processing site. Genes Dev. 6 (1992) 149–159. [PMID: 1730408]
3.  Cormack, R.S., Genereaux, J.L. and Mackie, G.A. RNase E activity is conferred by a single polypeptide: overexpression, purification, and properties of the ams/rne/hmp1 gene product. Proc. Natl. Acad. Sci. USA 90 (1993) 9006–9010. [PMID: 8415644]
4.  Vanzo, N.F., Li, Y.S., Py, B., Blum, E., Higgins, C.F., Raynal, L.C., Krisch, H.M. and Carpousis, A.J. Ribonuclease E organizes the protein interactions in the Escherichia coli RNA degradosome. Genes Dev. 12 (1998) 2770–2781. [PMID: 9732274]
5.  Steege, D.A. Emerging features of mRNA decay in bacteria. RNA 6 (2000) 1079–1090. [PMID: 10943888]
6.  Callaghan, A.J., Grossmann, J.G., Redko, Y.U., Ilag, L.L., Moncrieffe, M.C., Symmons, M.F., Robinson, C.V., McDowall, K.J. and Luisi, B.F. Quaternary structure and catalytic activity of the Escherichia coli ribonuclease E amino-terminal catalytic domain. Biochemistry 42 (2003) 13848–13855. [PMID: 14636052]
[EC 3.1.26.12 created 2008]
 
 
EC 3.4.11.24 – public review until 29 August 2008 [Last modified: 2008-08-01 12:13:01]
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.
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. [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. [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. [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. [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]
 
 


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