The Enzyme Database

Your query returned 11 entries.    printer_iconPrintable version



EC 3.5.1.11     
Accepted name: penicillin amidase
Reaction: penicillin + H2O = a carboxylate + 6-aminopenicillanate
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.
[EC 3.5.1.11 created 1961]
 
 
EC 3.5.1.110     
Accepted name: peroxyureidoacrylate/ureidoacrylate amidohydrolase
Reaction: (1) (Z)-3-ureidoacrylate peracid + H2O = (Z)-3-peroxyaminoacrylate + CO2 + NH3 (overall reaction)
(1a) (Z)-3-ureidoacrylate peracid + H2O = (Z)-3-peroxyaminoacrylate + carbamate
(1b) carbamate = CO2 + NH3 (spontaneous)
(2) (Z)-2-methylureidoacrylate peracid + H2O = (Z)-2-methylperoxyaminoacrylate + CO2 + NH3 (overall reaction)
(2a) (Z)-2-methylureidoacrylate peracid + H2O = (Z)-2-methylperoxyaminoacrylate + carbamate
(2b) carbamate = CO2 + NH3 (spontaneous)
Glossary: ureidoperacrylic acid = (Z)-3-ureidoacrylate peracid = (2Z)-3-(carbamoylamino)prop-2-eneperoxoic acid
(Z)-2-methylureidoperacrylic acid = (Z)-2-methylureidoacrylate peracid = (2Z)-3-(carbamoylamino)-2-methylprop-2-eneperoxoic acid
Other name(s): RutB
Systematic name: (Z)-3-ureidoacrylate peracid amidohydrolase
Comments: The enzyme also shows activity towards ureidoacrylate. Part of the Rut pyrimidine catabolic pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
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]
[EC 3.5.1.110 created 2012]
 
 
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]
[EC 3.5.1.111 created 2012]
 
 
EC 3.5.1.112     
Accepted name: 2′-N-acetylparomamine deacetylase
Reaction: 2′-N-acetylparomamine + H2O = paromamine + acetate
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]
[EC 3.5.1.112 created 2012]
 
 
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]
[EC 3.5.1.113 created 2012]
 
 
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
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]
[EC 3.5.1.114 created 2013]
 
 
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]
[EC 3.5.1.115 created 2013]
 
 
EC 3.5.1.116     
Accepted name: ureidoglycolate amidohydrolase
Reaction: (S)-ureidoglycolate + H2O = glyoxylate + 2 NH3 + CO2
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]
[EC 3.5.1.116 created 1992 as EC 3.5.3.19, transferred 2014 to EC 3.5.1.116]
 
 
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
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]
[EC 3.5.1.117 created 2014]
 
 
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
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
References:
1.  Seebeck, F.P. In vitro reconstitution of mycobacterial ergothioneine biosynthesis. J. Am. Chem. Soc. 132 (2010) 6632–6633. [DOI] [PMID: 20420449]
[EC 3.5.1.118 created 2015]
 
 
EC 3.5.1.119     
Accepted name: Pup amidohydrolase
Reaction: [prokaryotic ubiquitin-like protein]-L-glutamine + H2O = [prokaryotic ubiquitin-like protein]-L-glutamate + NH3
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]
[EC 3.5.1.119 created 2015]
 
 


Data © 2001–2018 IUBMB
Web site © 2005–2018 Andrew McDonald