EC |
3.5.1.11 |
Accepted name: |
penicillin amidase |
Reaction: |
penicillin + H2O = a carboxylate + 6-aminopenicillanate |
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For diagram of penicillin biosynthesis and metabolism, click here |
Other name(s): |
penicillin acylase; benzylpenicillin acylase; novozym 217; semacylase; α-acylamino-β-lactam acylhydrolase; ampicillin acylase |
Systematic name: |
penicillin amidohydrolase |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9014-06-6 |
References: |
1. |
Sakaguchi, K. and Murao, S. A preliminary report on a new enzyme, "penicillin-amidase". J. Agric. Chem. Soc. Jpn. 23 (1950) 411. |
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[EC 3.5.1.11 created 1961] |
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EC |
3.5.1.110 |
Accepted name: |
ureidoacrylate amidohydrolase |
Reaction: |
(1) (Z)-3-ureidoacrylate + H2O = (Z)-3-aminoacrylate + CO2 + NH3 (overall reaction) (1a) (Z)-3-ureidoacrylate + H2O = (Z)-3-aminoacrylate + carbamate (1b) carbamate = CO2 + NH3 (spontaneous) (2) (Z)-2-methylureidoacrylate + H2O = (Z)-2-methylaminoacrylate + CO2 + NH3 (overall reaction) (2a) (Z)-2-methylureidoacrylate + H2O = (Z)-2-methylaminoacrylate + carbamate (2b) carbamate = CO2 + NH3 (spontaneous)
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For diagram of pyrimidine catabolism, click here |
Glossary: |
(Z)-3-ureidoacrylate = (2Z)-3-(carbamoylamino)prop-2-enoate
(Z)-2-methylureidoacrylate = (2Z)-3-(carbamoylamino)-2-methylprop-2-enoate |
Other name(s): |
peroxyureidoacrylate/ureidoacrylate amidohydrolase; rutB (gene name); (Z)-3-ureidoacrylate peracid amidohydrolase |
Systematic name: |
(Z)-3-ureidoacrylate amidohydrolase |
Comments: |
The enzyme participates in the Rut pyrimidine catabolic pathway. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Kim, K.S., Pelton, J.G., Inwood, W.B., Andersen, U., Kustu, S. and Wemmer, D.E. The Rut pathway for pyrimidine degradation: novel chemistry and toxicity problems. J. Bacteriol. 192 (2010) 4089–4102. [DOI] [PMID: 20400551] |
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[EC 3.5.1.110 created 2012, modified 2020] |
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EC |
3.5.1.111 |
Accepted name: |
2-oxoglutaramate amidase |
Reaction: |
2-oxoglutaramate + H2O = 2-oxoglutarate + NH3 |
Glossary: |
2-oxoglutaramate = 2-ketoglutaramate = 5-amino-2,5-dioxopentanoate |
Other name(s): |
ω-amidase (ambiguous) |
Systematic name: |
5-amino-2,5-dioxopentanoate amidohydrolase |
Comments: |
The enzyme, which is highly specific for its substrate, participates in the nicotine degradation pathway of several Gram-positive bacteria. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Cobzaru, C., Ganas, P., Mihasan, M., Schleberger, P. and Brandsch, R. Homologous gene clusters of nicotine catabolism, including a new ω-amidase for α-ketoglutaramate, in species of three genera of Gram-positive bacteria. Res. Microbiol. 162 (2011) 285–291. [DOI] [PMID: 21288482] |
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[EC 3.5.1.111 created 2012] |
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EC |
3.5.1.112 |
Accepted name: |
2′-N-acetylparomamine deacetylase |
Reaction: |
2′-N-acetylparomamine + H2O = paromamine + acetate |
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For diagram of paromamine biosynthesis, click here |
Glossary: |
paromamine = (1R)-O4-(2-amino-2-deoxy-α-D-glucopyranosyl)-2-deoxy-streptamine |
Other name(s): |
btrD (gene name); neoL (gene name); kanN (gene name) |
Systematic name: |
2′-N-acetylparomamine hydrolase (acetate-forming) |
Comments: |
Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin, butirosin, neomycin and ribostamycin. The enzyme from the bacterium Streptomyces fradiae can also accept 2′′′-acetyl-6′′′-hydroxyneomycin C as substrate, cf. EC 3.5.1.113, 2′′′-acetyl-6′′′-hydroxyneomycin C deacetylase [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Truman, A.W., Huang, F., Llewellyn, N.M. and Spencer, J.B. Characterization of the enzyme BtrD from Bacillus circulans and revision of its functional assignment in the biosynthesis of butirosin. Angew. Chem. Int. Ed. Engl. 46 (2007) 1462–1464. [DOI] [PMID: 17226887] |
2. |
Yokoyama, K., Yamamoto, Y., Kudo, F. and Eguchi, T. Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function deacetylase in neomycin biosynthesis. ChemBioChem 9 (2008) 865–869. [DOI] [PMID: 18311744] |
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[EC 3.5.1.112 created 2012] |
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EC |
3.5.1.113 |
Accepted name: |
2′′′-acetyl-6′′′-hydroxyneomycin C deacetylase |
Reaction: |
2′′′-acetyl-6′′′-deamino-6′′′-hydroxyneomycin C + H2O = 6′′′-deamino-6′′′-hydroxyneomycin C + acetate |
Other name(s): |
neoL (gene name) |
Systematic name: |
2′′′-acetyl-6′′′-hydroxyneomycin C hydrolase (acetate-forming) |
Comments: |
Involved in the biosynthetic pathway of aminoglycoside antibiotics of the neomycin family. The enzyme from the bacterium Streptomyces fradiae also catalyses EC 3.5.1.112, 2′-N-acetylparomamine deacetylase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Yokoyama, K., Yamamoto, Y., Kudo, F. and Eguchi, T. Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function deacetylase in neomycin biosynthesis. ChemBioChem 9 (2008) 865–869. [DOI] [PMID: 18311744] |
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[EC 3.5.1.113 created 2012] |
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EC |
3.5.1.114 |
Accepted name: |
N-acyl-aromatic-L-amino acid amidohydrolase |
Reaction: |
(1) an N-acyl-aromatic-L-amino acid + H2O = an aromatic-L-amino acid + a carboxylate (2) an N-acetyl-L-cysteine-S-conjugate + H2O = an L-cysteine-S-conjugate + acetate |
Glossary: |
N-acetyl-L-cysteine-S-conjugate = mercapturic acid |
Other name(s): |
aminoacylase 3; aminoacylase III; ACY3 (gene name) |
Systematic name: |
N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming) |
Comments: |
This enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). It preferentially deacetylates Nα-acetylated aromatic amino acids and mercapturic acids (S-conjugates of N-acetyl-L-cysteine) that are usually not deacetylated by EC 3.5.1.14, N-acyl-aliphatic-L-amino acid amidohydrolase. The enzyme is significantly activated by Co2+ and Ni2+ [3]. Some bacterial aminoacylases demonstrate substrate specificity for both EC 3.5.1.14 and EC 3.5.1.114. cf. EC 3.5.1.14, N-acyl-aliphatic-L-amino acid amidohydrolase and EC 3.5.1.15, aspartoacylase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Pushkin, A., Carpenito, G., Abuladze, N., Newman, D., Tsuprun, V., Ryazantsev, S., Motemoturu, S., Sassani, P., Solovieva, N., Dukkipati, R. and Kurtz, I. Structural characterization, tissue distribution, and functional expression of murine aminoacylase III. Am. J. Physiol. Cell Physiol. 286 (2004) C848–C856. [DOI] [PMID: 14656720] |
2. |
Newman, D., Abuladze, N., Scholz, K., Dekant, W., Tsuprun, V., Ryazantsev, S., Bondar, G., Sassani, P., Kurtz, I. and Pushkin, A. Specificity of aminoacylase III-mediated deacetylation of mercapturic acids. Drug Metab. Dispos. 35 (2007) 43–50. [DOI] [PMID: 17012540] |
3. |
Tsirulnikov, K., Abuladze, N., Newman, D., Ryazantsev, S., Wolak, T., Magilnick, N., Koag, M.C., Kurtz, I. and Pushkin, A. Mouse aminoacylase 3: a metalloenzyme activated by cobalt and nickel. Biochim. Biophys. Acta 1794 (2009) 1049–1057. [DOI] [PMID: 19362172] |
4. |
Hsieh, J.M., Tsirulnikov, K., Sawaya, M.R., Magilnick, N., Abuladze, N., Kurtz, I., Abramson, J. and Pushkin, A. Structures of aminoacylase 3 in complex with acetylated substrates. Proc. Natl. Acad. Sci. USA 107 (2010) 17962–17967. [DOI] [PMID: 20921362] |
5. |
Tsirulnikov, K., Abuladze, N., Bragin, A., Faull, K., Cascio, D., Damoiseaux, R., Schibler, M.J. and Pushkin, A. Inhibition of aminoacylase 3 protects rat brain cortex neuronal cells from the toxicity of 4-hydroxy-2-nonenal mercapturate and 4-hydroxy-2-nonenal. Toxicol. Appl. Pharmacol. 263 (2012) 303–314. [DOI] [PMID: 22819785] |
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[EC 3.5.1.114 created 2013] |
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EC |
3.5.1.115 |
Accepted name: |
mycothiol S-conjugate amidase |
Reaction: |
a mycothiol S-conjugate + H2O = an N-acetyl L-cysteine-S-conjugate + 1-O-(2-amino-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol |
Glossary: |
mycothiol = 1-O-[2-(N2-acetyl-L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-1D-myo-inositol
N-acetyl L-cysteine-S-conjugate = mercapturic acid |
Other name(s): |
MCA |
Systematic name: |
mycothiol S-conjugate 1D-myo-inositol 2-amino-2-deoxy-α-D-glucopyranosyl-hydrolase |
Comments: |
The enzyme that is found in actinomycetes is involved in the detoxification of oxidizing agents and electrophilic antibiotics. The enzyme has low activity with 1-O-(2-acetamido-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol as substrate (cf. EC 3.5.1.103, N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-α-D-glucopyranoside deacetylase) [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Newton, G.L., Av-Gay, Y. and Fahey, R.C. A novel mycothiol-dependent detoxification pathway in mycobacteria involving mycothiol S-conjugate amidase. Biochemistry 39 (2000) 10739–10746. [DOI] [PMID: 10978158] |
2. |
Steffek, M., Newton, G.L., Av-Gay, Y. and Fahey, R.C. Characterization of Mycobacterium tuberculosis mycothiol S-conjugate amidase. Biochemistry 42 (2003) 12067–12076. [DOI] [PMID: 14556638] |
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[EC 3.5.1.115 created 2013] |
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EC |
3.5.1.116 |
Accepted name: |
ureidoglycolate amidohydrolase |
Reaction: |
(S)-ureidoglycolate + H2O = glyoxylate + 2 NH3 + CO2 |
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For diagram of AMP catabolism, click here |
Other name(s): |
ureidoglycolate hydrolase; UAH (gene name) |
Systematic name: |
(S)-ureidoglycolate amidohydrolase (decarboxylating) |
Comments: |
This plant enzyme is involved in the degradation of ureidoglycolate, an intermediate of purine degradation. Not to be confused with EC 4.3.2.3, ureidoglycolate lyase, which releases urea rather than ammonia. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 115629-07-7 |
References: |
1. |
Winkler, R.G., Blevins, D.G. and Randall, D.D. Ureide catabolism in soybeans. III. Ureidoglycolate amidohydrolase and allantoate amidohydrolase are activities of an allantoate degrading enzyme complex. Plant Physiol. 86 (1988) 1084–1088. [PMID: 16666035] |
2. |
Wells, X.E. and Lees, E.M. Ureidoglycolate amidohydrolase from developing French bean fruits (Phaseolus vulgaris [L.].). Arch. Biochem. Biophys. 287 (1991) 151–159. [DOI] [PMID: 1910298] |
3. |
Werner, A.K., Romeis, T. and Witte, C.P. Ureide catabolism in Arabidopsis thaliana and Escherichia coli. Nat. Chem. Biol. 6 (2010) 19–21. [DOI] [PMID: 19935661] |
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[EC 3.5.1.116 created 1992 as EC 3.5.3.19, transferred 2014 to EC 3.5.1.116] |
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EC |
3.5.1.117 |
Accepted name: |
6-aminohexanoate-oligomer endohydrolase |
Reaction: |
[N-(6-aminohexanoyl)]n + H2O = [N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x |
Other name(s): |
endo-type 6-aminohexanoate oligomer hydrolase; Ahx endo-type-oligomer hydrolase; 6-aminohexanoate oligomer hydrolase; Ahx-oligomer hydrolase; nylon hydrolase; nylon-oligomer hydrolase; NylC; nylon-6 hydrolase (ambiguous) |
Systematic name: |
6-aminohexanoate oligomer endoamidohydrolase |
Comments: |
The enzyme is involved in degradation of nylon-6 oligomers. It degrades linear or cyclic oligomers of poly(6-aminohexanoate) with a degree of polymerization greater than three (n > 3) by endo-type cleavage, to oligomers of a length of two or more (2 ≤ x < n). It shows negligible activity with N-(6-aminohexanoyl)-6-aminohexanoate (cf. EC 3.5.1.46, 6-aminohexanoate-oligomer exo hydrolase) or with 1,8-diazacyclotetradecane-2,9-dione (cf. EC 3.5.2.12, 6-aminohexanoate-cyclic-dimer hydrolase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Kakudo, S., Negoro, S., Urabe, I. and Okada, H. Nylon oligomer degradation gene, nylC, on plasmid pOAD2 from a Flavobacterium strain encodes endo-type 6-aminohexanoate oligomer hydrolase: purification and characterization of the nylC gene product. Appl. Environ. Microbiol. 59 (1993) 3978–3980. [PMID: 8285701] |
2. |
Yasuhira, K., Tanaka, Y., Shibata, H., Kawashima, Y., Ohara, A., Kato, D., Takeo, M. and Negoro, S. 6-Aminohexanoate oligomer hydrolases from the alkalophilic bacteria Agromyces sp. strain KY5R and Kocuria sp. strain KY2. Appl. Environ. Microbiol. 73 (2007) 7099–7102. [DOI] [PMID: 17827307] |
3. |
Negoro, S., Shibata, N., Tanaka, Y., Yasuhira, K., Shibata, H., Hashimoto, H., Lee, Y.H., Oshima, S., Santa, R., Oshima, S., Mochiji, K., Goto, Y., Ikegami, T., Nagai, K., Kato, D., Takeo, M. and Higuchi, Y. Three-dimensional structure of nylon hydrolase and mechanism of nylon-6 hydrolysis. J. Biol. Chem. 287 (2012) 5079–5090. [DOI] [PMID: 22187439] |
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[EC 3.5.1.117 created 2014] |
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EC |
3.5.1.118 |
Accepted name: |
γ-glutamyl hercynylcysteine S-oxide hydrolase |
Reaction: |
γ-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O = S-(hercyn-2-yl)-L-cysteine S-oxide + L-glutamate |
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For diagram of ergothioneine and ovothiol biosynthesis, click here |
Glossary: |
hercynine = Nα,Nα,Nα-trimethyl-L-histidine = 3-(1H-imidazol-5-yl)-2-(trimethylamino)propanoate
S-(hercyn-2-yl)-L-cysteine S-oxide = S-(N,N,N-trimethyl-L-histidin-2-yl)-L-cysteine S-oxide |
Other name(s): |
EgtC |
Systematic name: |
γ-glutamyl-S-(hercyn-2-yl)cysteine S-oxide amidohydrolase |
Comments: |
The enzyme is part of the biosynthesis pathway of ergothioneine in mycobacteria. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Seebeck, F.P. In vitro reconstitution of mycobacterial ergothioneine biosynthesis. J. Am. Chem. Soc. 132 (2010) 6632–6633. [DOI] [PMID: 20420449] |
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[EC 3.5.1.118 created 2015] |
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EC |
3.5.1.119 |
Accepted name: |
Pup amidohydrolase |
Reaction: |
[prokaryotic ubiquitin-like protein]-L-glutamine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + NH3
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Other name(s): |
dop (gene name); Pup deamidase; depupylase/deamidase; DPUP; depupylase |
Systematic name: |
[prokaryotic ubiquitin-like protein]-L-glutamine amidohydrolase |
Comments: |
The enzyme has been characterized from the bacterium Mycobacterium tuberculosis. It catalyses the hydrolysis of the amido group of the C-terminal glutamine of prokaryotic ubiquitin-like protein (Pup), thus activating it for ligation to target proteins, a process catalysed by EC 6.3.1.19, prokaryotic ubiquitin-like protein ligase. The reaction requires ATP as cofactor but not its hydrolysis. The enzyme also catalyses the hydrolytic cleavage of the bond formed by the ligase, between an ε-amino group of a lysine residue of the target protein and the γ-carboxylate of the C-terminal glutamate of the prokaryotic ubiquitin-like protein. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Striebel, F., Imkamp, F., Sutter, M., Steiner, M., Mamedov, A. and Weber-Ban, E. Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes. Nat. Struct. Mol. Biol. 16 (2009) 647–651. [DOI] [PMID: 19448618] |
2. |
Burns, K.E., Cerda-Maira, F.A., Wang, T., Li, H., Bishai, W.R. and Darwin, K.H. "Depupylation" of prokaryotic ubiquitin-like protein from mycobacterial proteasome substrates. Mol. Cell 39 (2010) 821–827. [DOI] [PMID: 20705495] |
3. |
Striebel, F., Imkamp, F., Özcelik, D. and Weber-Ban, E. Pupylation as a signal for proteasomal degradation in bacteria. Biochim. Biophys. Acta 1843 (2014) 103–113. [DOI] [PMID: 23557784] |
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[EC 3.5.1.119 created 2015] |
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