EC |
3.5.1.101 |
Accepted name: |
L-proline amide hydrolase |
Reaction: |
(1) (S)-piperidine-2-carboxamide + H2O = (S)-piperidine-2-carboxylate + NH3 (2) L-prolinamide + H2O = L-proline + NH3 |
Glossary: |
L-pipecolate = piperidine-2-carboxylate |
Other name(s): |
S-stereoselective piperazine-2-tert-butylcarboxamide hydrolase; LaaA; L-amino acid amidase |
Systematic name: |
(S)-piperidine-2-carboxamide amidohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Komeda, H., Harada, H., Washika, S., Sakamoto, T., Ueda, M. and Asano, Y. S-stereoselective piperazine-2-tert-butylcarboxamide hydrolase from Pseudomonas azotoformans IAM 1603 is a novel L-amino acid amidase. Eur. J. Biochem. 271 (2004) 1465–1475. [DOI] [PMID: 15066172] |
|
[EC 3.5.1.101 created 2009] |
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|
|
|
EC |
3.5.1.102 |
Accepted name: |
2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5′-monophosphate deformylase |
Reaction: |
2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + H2O = 2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + formate |
Other name(s): |
ArfB |
Systematic name: |
2-amino-5-formylamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one amidohydrolase |
Comments: |
The enzyme catalyses the second step in archaeal riboflavin and 7,8-didemethyl-8-hydroxy-5-deazariboflavin biosynthesis. The first step is catalysed by EC 3.5.4.29 (GTP cyclohydrolase IIa). The bacterial enzyme, EC 3.5.4.25 (GTP cyclohydrolase II) catalyses both reactions. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Grochowski, L.L., Xu, H. and White, R.H. An iron(II) dependent formamide hydrolase catalyzes the second step in the archaeal biosynthetic pathway to riboflavin and 7,8-didemethyl-8-hydroxy-5-deazariboflavin. Biochemistry 48 (2009) 4181–4188. [DOI] [PMID: 19309161] |
|
[EC 3.5.1.102 created 2010, modified 2011] |
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|
|
|
EC |
3.5.1.103 |
Accepted name: |
N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-α-D-glucopyranoside deacetylase |
Reaction: |
1-O-(2-acetamido-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol + H2O = 1-O-(2-amino-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol + acetate |
|
For diagram of mycothiol biosynthesis, click here |
Glossary: |
mycothiol = 1-O-[2-(N2-acetyl-L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-1D-myo-inositol |
Other name(s): |
MshB |
Systematic name: |
1-(2-acetamido-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol acetylhydrolase |
Comments: |
This enzyme is considered the key enzyme and rate limiting step in the mycothiol biosynthesis pathway [1]. In addition to acetylase activity, the enzyme possesses weak activity of EC 3.5.1.115, mycothiol S-conjugate amidase, and shares sequence similarity with that enzyme [2]. The enzyme requires a divalent transition metal ion for activity, believed to be Zn2+ [3]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Rawat, M., Kovacevic, S., Billman-Jacobe, H. and Av-Gay, Y. Inactivation of mshB, a key gene in the mycothiol biosynthesis pathway in Mycobacterium smegmatis. Microbiology 149 (2003) 1341–1349. [DOI] [PMID: 12724395] |
2. |
Newton, G.L., Av-Gay, Y. and Fahey, R.C. N-Acetyl-1-D-myo-inosityl-2-amino-2-deoxy-α-D-glucopyranoside deacetylase (MshB) is a key enzyme in mycothiol biosynthesis. J. Bacteriol. 182 (2000) 6958–6963. [DOI] [PMID: 11092856] |
3. |
Maynes, J.T., Garen, C., Cherney, M.M., Newton, G., Arad, D., Av-Gay, Y., Fahey, R.C. and James, M.N. The crystal structure of 1-D-myo-inosityl 2-acetamido-2-deoxy-α-D-glucopyranoside deacetylase (MshB) from Mycobacterium tuberculosis reveals a zinc hydrolase with a lactate dehydrogenase fold. J. Biol. Chem. 278 (2003) 47166–47170. [DOI] [PMID: 12958317] |
|
[EC 3.5.1.103 created 2010] |
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|
|
|
EC |
3.5.1.104 |
Accepted name: |
peptidoglycan-N-acetylglucosamine deacetylase |
Reaction: |
peptidoglycan-N-acetyl-D-glucosamine + H2O = peptidoglycan-D-glucosamine + acetate |
Other name(s): |
HP310; PgdA; SpPgdA; BC1960; peptidoglycan deacetylase; N-acetylglucosamine deacetylase; peptidoglycan GlcNAc deacetylase; peptidoglycan N-acetylglucosamine deacetylase; PG N-deacetylase |
Systematic name: |
peptidoglycan-N-acetylglucosamine amidohydrolase |
Comments: |
Modification of peptidoglycan by N-deacetylation is an important factor in virulence of Helicobacter pylori, Listeria monocytogenes and Streptococcus suis [4-6]. The enzyme from Streptococcus pneumoniae is a metalloenzyme using a His-His-Asp zinc-binding triad with a nearby aspartic acid and histidine acting as the catalytic base and acid, respectively [3]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Psylinakis, E., Boneca, I.G., Mavromatis, K., Deli, A., Hayhurst, E., Foster, S.J., Varum, K.M. and Bouriotis, V. Peptidoglycan N-acetylglucosamine deacetylases from Bacillus cereus, highly conserved proteins in Bacillus anthracis. J. Biol. Chem. 280 (2005) 30856–30863. [DOI] [PMID: 15961396] |
2. |
Tsalafouta, A., Psylinakis, E., Kapetaniou, E.G., Kotsifaki, D., Deli, A., Roidis, A., Bouriotis, V. and Kokkinidis, M. Purification, crystallization and preliminary X-ray analysis of the peptidoglycan N-acetylglucosamine deacetylase BC1960 from Bacillus cereus in the presence of its substrate (GlcNAc)6. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 (2008) 203–205. [DOI] [PMID: 18323609] |
3. |
Blair, D.E., Schuttelkopf, A.W., MacRae, J.I. and van Aalten, D.M. Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factor. Proc. Natl. Acad. Sci. USA 102 (2005) 15429–15434. [DOI] [PMID: 16221761] |
4. |
Wang, G., Olczak, A., Forsberg, L.S. and Maier, R.J. Oxidative stress-induced peptidoglycan deacetylase in Helicobacter pylori. J. Biol. Chem. 284 (2009) 6790–6800. [DOI] [PMID: 19147492] |
5. |
Popowska, M., Kusio, M., Szymanska, P. and Markiewicz, Z. Inactivation of the wall-associated de-N-acetylase (PgdA) of Listeria monocytogenes results in greater susceptibility of the cells to induced autolysis. J. Microbiol. Biotechnol. 19 (2009) 932–945. [PMID: 19809250] |
6. |
Fittipaldi, N., Sekizaki, T., Takamatsu, D., de la Cruz Domínguez-Punaro, M., Harel, J., Bui, N.K., Vollmer, W. and Gottschalk, M. Significant contribution of the pgdA gene to the virulence of Streptococcus suis. Mol. Microbiol. 70 (2008) 1120–1135. [DOI] [PMID: 18990186] |
|
[EC 3.5.1.104 created 2010] |
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|
EC |
3.5.1.105 |
Accepted name: |
chitin disaccharide deacetylase |
Reaction: |
N,N′-diacetylchitobiose + H2O = N-acetyl-β-D-glucosaminyl-(1→4)-D-glucosamine + acetate |
Glossary: |
N,N′-diacetylchitobiose = N-acetyl-β-D-glucosaminyl-(1→4)-N-acetyl-D-glucosamine |
Other name(s): |
chitobiose amidohydolase; COD; chitin oligosaccharide deacetylase; chitin oligosaccharide amidohydolase; 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-β-D-glucopyranosyl]-2-deoxy-D-glucopyranose acetylhydrolase |
Systematic name: |
N,N′-diacetylchitobiose acetylhydrolase |
Comments: |
Chitin oligosaccharide deacetylase is a key enzyme in the chitin catabolic cascade of chitinolytic Vibrio strains. Besides being a nutrient, the heterodisaccharide product 4-O-(N-acetyl-β-D-glucosaminyl)-D-glucosamine is a unique inducer of chitinase production in Vibrio parahemolyticus [2]. In contrast to EC 3.5.1.41 (chitin deacetylase) this enzyme is specific for the chitin disaccharide [1,3]. It also deacetylates the chitin trisaccharide with lower efficiency [3]. No activity with higher polymers of GlcNAc [1,3]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Kadokura, K., Rokutani, A., Yamamoto, M., Ikegami, T., Sugita, H., Itoi, S., Hakamata, W., Oku, T. and Nishio, T. Purification and characterization of Vibrio parahaemolyticus extracellular chitinase and chitin oligosaccharide deacetylase involved in the production of heterodisaccharide from chitin. Appl. Microbiol. Biotechnol. 75 (2007) 357–365. [DOI] [PMID: 17334758] |
2. |
Hirano, T., Kadokura, K., Ikegami, T., Shigeta, Y., Kumaki, Y., Hakamata, W., Oku, T. and Nishio, T. Heterodisaccharide 4-O-(N-acetyl-β-D-glucosaminyl)-D-glucosamine is a specific inducer of chitinolytic enzyme production in Vibrios harboring chitin oligosaccharide deacetylase genes. Glycobiology 19 (2009) 1046–1053. [DOI] [PMID: 19553519] |
3. |
Ohishi, K., Yamagishi, M., Ohta, T., Motosugi, M., Izumida, H., Sano, H., Adachi, K., Miwa, T. Purification and properties of two deacetylases produced by Vibrio alginolyticus H-8. Biosci. Biotechnol. Biochem. 61 (1997) 1113–1117. |
4. |
Ohishi, K., Murase, K., Ohta, T. and Etoh, H. Cloning and sequencing of the deacetylase gene from Vibrio alginolyticus H-8. J. Biosci. Bioeng. 90 (2000) 561–563. [DOI] [PMID: 16232910] |
|
[EC 3.5.1.105 created 2010] |
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|
EC |
3.5.1.106 |
Accepted name: |
N-formylmaleamate deformylase |
Reaction: |
N-formylmaleamic acid + H2O = maleamate + formate |
Other name(s): |
NicD |
Systematic name: |
N-formylmaleamic acid amidohydrolase |
Comments: |
The reaction is involved in the aerobic catabolism of nicotinic acid. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc |
References: |
1. |
Jimenez, J.I., Canales, A., Jimenez-Barbero, J., Ginalski, K., Rychlewski, L., Garcia, J.L. and Diaz, E. Deciphering the genetic determinants for aerobic nicotinic acid degradation: the nic cluster from Pseudomonas putida KT2440. Proc. Natl. Acad. Sci. USA 105 (2008) 11329–11334. [DOI] [PMID: 18678916] |
|
[EC 3.5.1.106 created 2010] |
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|
EC |
3.5.1.107 |
Accepted name: |
maleamate amidohydrolase |
Reaction: |
maleamate + H2O = maleate + NH3 |
Other name(s): |
NicF |
Systematic name: |
maleamate amidohydrolase |
Comments: |
The reaction is involved in the aerobic catabolism of nicotinic acid. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Jimenez, J.I., Canales, A., Jimenez-Barbero, J., Ginalski, K., Rychlewski, L., Garcia, J.L. and Diaz, E. Deciphering the genetic determinants for aerobic nicotinic acid degradation: the nic cluster from Pseudomonas putida KT2440. Proc. Natl. Acad. Sci. USA 105 (2008) 11329–11334. [DOI] [PMID: 18678916] |
|
[EC 3.5.1.107 created 2010] |
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|
EC |
3.5.1.108 |
Accepted name: |
UDP-3-O-acyl-N-acetylglucosamine deacetylase |
Reaction: |
a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-α-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-α-D-glucosamine + acetate |
|
For diagram of lipid IVA biosynthesis, click here |
Other name(s): |
LpxC protein; LpxC enzyme; LpxC deacetylase; deacetylase LpxC; UDP-3-O-acyl-GlcNAc deacetylase; UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase; UDP-(3-O-acyl)-N-acetylglucosamine deacetylase; UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase; UDP-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine deacetylase; UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetylglucosamine amidohydrolase |
Systematic name: |
UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-α-D-glucosamine amidohydrolase |
Comments: |
A zinc protein. The enzyme catalyses a committed step in the biosynthesis of lipid A. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Hernick, M., Gennadios, H.A., Whittington, D.A., Rusche, K.M., Christianson, D.W. and Fierke, C.A. UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism. J. Biol. Chem. 280 (2005) 16969–16978. [DOI] [PMID: 15705580] |
2. |
Jackman, J.E., Raetz, C.R. and Fierke, C.A. UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme. Biochemistry 38 (1999) 1902–1911. [DOI] [PMID: 10026271] |
3. |
Hyland, S.A., Eveland, S.S. and Anderson, M.S. Cloning, expression, and purification of UDP-3-O-acyl-GlcNAc deacetylase from Pseudomonas aeruginosa: a metalloamidase of the lipid A biosynthesis pathway. J. Bacteriol. 179 (1997) 2029–2037. [DOI] [PMID: 9068651] |
4. |
Wang, W., Maniar, M., Jain, R., Jacobs, J., Trias, J. and Yuan, Z. A fluorescence-based homogeneous assay for measuring activity of UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase. Anal. Biochem. 290 (2001) 338–346. [DOI] [PMID: 11237337] |
5. |
Whittington, D.A., Rusche, K.M., Shin, H., Fierke, C.A. and Christianson, D.W. Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis. Proc. Natl. Acad. Sci. USA 100 (2003) 8146–8150. [DOI] [PMID: 12819349] |
6. |
Mochalkin, I., Knafels, J.D. and Lightle, S. Crystal structure of LpxC from Pseudomonas aeruginosa complexed with the potent BB-78485 inhibitor. Protein Sci. 17 (2008) 450–457. [DOI] [PMID: 18287278] |
|
[EC 3.5.1.108 created 2010, modified 2021] |
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|
EC |
3.5.1.109 |
Accepted name: |
sphingomyelin deacylase |
Reaction: |
(1) an N-acyl-sphingosylphosphorylcholine + H2O = a fatty acid + sphingosylphosphorylcholine
(2) a D-glucosyl-N-acylsphingosine + H2O = a fatty acid + D-glucosyl-sphingosine |
Glossary: |
sphingomyelin = N-acyl-sphingosylphosphorylcholine
D-glucosyl-N-acylsphingosine = glucosylceramide |
Other name(s): |
SM deacylase; GcSM deacylase; glucosylceramide sphingomyelin deacylase; sphingomyelin glucosylceramide deacylase; SM glucosylceramide GCer deacylase; SM-GCer deacylase; SMGCer deacylase |
Systematic name: |
N-acyl-sphingosylphosphorylcholine amidohydrolase |
Comments: |
The enzyme is involved in the sphingolipid metabolism in the epidermis. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Hara, J., Higuchi, K., Okamoto, R., Kawashima, M. and Imokawa, G. High-expression of sphingomyelin deacylase is an important determinant of ceramide deficiency leading to barrier disruption in atopic dermatitis. J. Invest. Dermatol. 115 (2000) 406–413. [DOI] [PMID: 10951276] |
2. |
Higuchi, K., Hara, J., Okamoto, R., Kawashima, M. and Imokawa, G. The skin of atopic dermatitis patients contains a novel enzyme, glucosylceramide sphingomyelin deacylase, which cleaves the N-acyl linkage of sphingomyelin and glucosylceramide. Biochem. J. 350 (2000) 747–756. [PMID: 10970788] |
3. |
Ishibashi, M., Arikawa, J., Okamoto, R., Kawashima, M., Takagi, Y., Ohguchi, K. and Imokawa, G. Abnormal expression of the novel epidermal enzyme, glucosylceramide deacylase, and the accumulation of its enzymatic reaction product, glucosylsphingosine, in the skin of patients with atopic dermatitis. Lab. Invest. 83 (2003) 397–408. [PMID: 12649340] |
|
[EC 3.5.1.109 created 2011] |
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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)
|
|
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] |
|
[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 |
|
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] |
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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] |
|
[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] |
|
[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, 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] |
|
[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, PDB |
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] |
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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
|
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] |
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|
EC
|
3.5.1.120
|
Transferred entry: | 2-aminomuconate deaminase (2-hydroxymuconate-forming). Now EC 3.5.99.11, 2-aminomuconate deaminase (2-hydroxymuconate-forming)
|
[EC 3.5.1.120 created 2016, deleted 2017] |
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|
|
|
EC |
3.5.1.121 |
Accepted name: |
protein N-terminal asparagine amidohydrolase |
Reaction: |
N-terminal L-asparaginyl-[protein] + H2O = N-terminal L-aspartyl-[protein] + NH3 |
Other name(s): |
NTAN1 (gene name) |
Systematic name: |
protein N-terminal asparagine amidohydrolase |
Comments: |
This enzyme participates in the eukaryotic ubiquitin-dependent Arg/N-end rule pathway of protein degradation, promoting the turnover of intracellular proteins that initiate with Met-Asn. Following the acetylation and removal of the initiator methionine, the exposed N-terminal asparagine is deaminated, resulting in its conversion to L-aspartate. The latter serves as a substrate for EC 2.3.2.8, arginyltransferase, making the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Stewart, A.E., Arfin, S.M. and Bradshaw, R.A. Protein NH2-terminal asparagine deamidase. Isolation and characterization of a new enzyme. J. Biol. Chem. 269 (1994) 23509–23517. [PMID: 8089117] |
2. |
Grigoryev, S., Stewart, A.E., Kwon, Y.T., Arfin, S.M., Bradshaw, R.A., Jenkins, N.A., Copeland, N.G. and Varshavsky, A. A mouse amidase specific for N-terminal asparagine. The gene, the enzyme, and their function in the N-end rule pathway. J. Biol. Chem. 271 (1996) 28521–28532. [DOI] [PMID: 8910481] |
3. |
Cantor, J.R., Stone, E.M. and Georgiou, G. Expression and biochemical characterization of the human enzyme N-terminal asparagine amidohydrolase. Biochemistry 50 (2011) 3025–3033. [DOI] [PMID: 21375249] |
|
[EC 3.5.1.121 created 2016] |
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|
EC |
3.5.1.122 |
Accepted name: |
protein N-terminal glutamine amidohydrolase |
Reaction: |
N-terminal L-glutaminyl-[protein] + H2O = N-terminal L-glutamyl-[protein] + NH3 |
Other name(s): |
NTAQ1 (gene name) |
Systematic name: |
protein N-terminal glutamine amidohydrolase |
Comments: |
This enzyme participates in the eukaryotic ubiquitin-dependent Arg/N-end rule pathway of protein degradation, promoting the turnover of intracellular proteins that initiate with Met-Gln. Following the acetylation and removal of the initiator methionine, the exposed N-terminal glutamine is deaminated, resulting in its conversion to L-glutamate. The latter serves as a substrate for EC 2.3.2.8, arginyltransferase, making the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Wang, H., Piatkov, K.I., Brower, C.S. and Varshavsky, A. Glutamine-specific N-terminal amidase, a component of the N-end rule pathway. Mol. Cell 34 (2009) 686–695. [DOI] [PMID: 19560421] |
|
[EC 3.5.1.122 created 2016] |
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|
|
EC |
3.5.1.123 |
Accepted name: |
γ-glutamylanilide hydrolase |
Reaction: |
N5-phenyl-L-glutamine + H2O = L-glutamate + aniline |
Glossary: |
γ-glutamylanilide = N5-phenyl-L-glutamine |
Other name(s): |
atdA2 (gene name) |
Systematic name: |
N5-phenyl-L-glutamine amidohydrolase |
Comments: |
The enzyme, characterized from the bacterium Acinetobacter sp. YAA, catalyses the opposite reaction from that catalysed by EC 6.3.1.18, γ-glutamylanilide synthase, which is part of an aniline degradation pathway. Its purpose is likely to maintain a low concentration of N5-phenyl-L-glutamine, which is potentially toxic. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Takeo, M., Ohara, A., Sakae, S., Okamoto, Y., Kitamura, C., Kato, D. and Negoro, S. Function of a glutamine synthetase-like protein in bacterial aniline oxidation via γ-glutamylanilide. J. Bacteriol. 195 (2013) 4406–4414. [DOI] [PMID: 23893114] |
|
[EC 3.5.1.123 created 2016] |
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|
EC |
3.5.1.124 |
Accepted name: |
protein deglycase |
Reaction: |
(1) an Nω-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O = a [protein]-L-arginine + lactate (2) an N6-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O = a [protein]-L-lysine + lactate (3) an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O = a [protein]-L-cysteine + lactate |
Glossary: |
2-oxopropanal = methylglyoxal |
Other name(s): |
PARK7 (gene name); DJ-1 protein; yhbO (gene name); yajL (gene name); glyoxylase III (incorrect) |
Systematic name: |
a [protein]-L-amino acid-1-hydroxypropan-2-one hydrolase [(R)-lactate-forming] |
Comments: |
The enzyme, previously thought to be a glyoxalase, acts on glycated L-arginine, L-lysine, and L-cysteine residues within proteins that have been attacked and modified by glyoxal or 2-oxopropanal. The attack forms hemithioacetal in the case of cysteines and aminocarbinols in the case of arginines and lysines. The enzyme repairs the amino acids, releasing glycolate or lactate (70-80% (S)-lactate and 20-30% (R)-lactate), depending on whether the attacking agent was glyoxal or 2-oxopropanal, respectively [3,4]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Misra, K., Banerjee, A.B., Ray, S. and Ray, M. Glyoxalase III from Escherichia coli: a single novel enzyme for the conversion of methylglyoxal into D-lactate without reduced glutathione. Biochem. J. 305 (1995) 999–1003. [PMID: 7848303] |
2. |
Subedi, K.P., Choi, D., Kim, I., Min, B. and Park, C. Hsp31 of Escherichia coli K-12 is glyoxalase III. Mol. Microbiol. 81 (2011) 926–936. [DOI] [PMID: 21696459] |
3. |
Richarme, G., Mihoub, M., Dairou, J., Bui, L.C., Leger, T. and Lamouri, A. Parkinsonism-associated protein DJ-1/Park7 is a major protein deglycase that repairs methylglyoxal- and glyoxal-glycated cysteine, arginine, and lysine residues. J. Biol. Chem. 290 (2015) 1885–1897. [DOI] [PMID: 25416785] |
4. |
Mihoub, M., Abdallah, J., Gontero, B., Dairou, J. and Richarme, G. The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal. Biochem. Biophys. Res. Commun. 463 (2015) 1305–1310. [DOI] [PMID: 26102038] |
5. |
Abdallah, J., Mihoub, M., Gautier, V. and Richarme, G. The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal. Biochem. Biophys. Res. Commun. 470 (2016) 282–286. [DOI] [PMID: 26774339] |
|
[EC 3.5.1.124 created 2016] |
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|
EC |
3.5.1.125 |
Accepted name: |
N2-acetyl-L-2,4-diaminobutanoate deacetylase |
Reaction: |
(2S)-2-acetamido-4-aminobutanoate + H2O = L-2,4-diaminobutanoate + acetate |
Other name(s): |
doeB (gene name) |
Systematic name: |
(2S)-2-acetamido-4-aminobutanoate amidohydrolase |
Comments: |
The enzyme, found in bacteria, has no activity with (2S)-4-acetamido-2-aminobutanoate (cf. EC 3.5.4.44, ectoine hydrolase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Schwibbert, K., Marin-Sanguino, A., Bagyan, I., Heidrich, G., Lentzen, G., Seitz, H., Rampp, M., Schuster, S.C., Klenk, H.P., Pfeiffer, F., Oesterhelt, D. and Kunte, H.J. A blueprint of ectoine metabolism from the genome of the industrial producer Halomonas elongata DSM 2581 T. Environ. Microbiol. 13 (2011) 1973–1994. [DOI] [PMID: 20849449] |
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[EC 3.5.1.125 created 2017] |
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|
|
EC |
3.5.1.126 |
Accepted name: |
oxamate amidohydrolase |
Reaction: |
oxamate + H2O = oxalate + NH3 |
Other name(s): |
HpxW |
Systematic name: |
oxamate amidohydrolase |
Comments: |
The enzyme has been characterized from the bacterium Klebsiella pneumoniae. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Hicks, K.A. and Ealick, S.E. Biochemical and structural characterization of Klebsiella pneumoniae oxamate amidohydrolase in the uric acid degradation pathway. Acta Crystallogr D Struct Biol 72 (2016) 808–816. [DOI] [PMID: 27303801] |
|
[EC 3.5.1.126 created 2017] |
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|
EC |
3.5.1.127 |
Accepted name: |
jasmonoyl-L-amino acid hydrolase |
Reaction: |
a jasmonoyl-L-amino acid + H2O = jasmonate + an L-amino acid |
Glossary: |
tuberonic acid = 12-hydroxyjasmonate = {(1R,2R)-2-[(2Z)-5-hydroxypent-2-enyl]-3-oxo-cyclopentyl}acetate
jasmonate = {(1R,2R)-3-oxo-2-[(2Z)-pent-2-enyl]cyclopentyl}acetate |
Other name(s): |
IAR3 (gene name); ILL4 (gene name); ILL6 (gene name) |
Systematic name: |
jasmonoyl-L-amino acid amidohydrolase |
Comments: |
This entry includes a family of enzymes that recyle jasmonoyl-amino acid conjugates back to jasmonates. The enzymes from Arabidopsis thaliana have been shown to also act on 12-hydroxyjasmonoyl-L-isoleucine, generating tuberonic acid. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Widemann, E., Miesch, L., Lugan, R., Holder, E., Heinrich, C., Aubert, Y., Miesch, M., Pinot, F. and Heitz, T. The amidohydrolases IAR3 and ILL6 contribute to jasmonoyl-isoleucine hormone turnover and generate 12-hydroxyjasmonic acid upon wounding in Arabidopsis leaves. J. Biol. Chem. 288 (2013) 31701–31714. [DOI] [PMID: 24052260] |
|
[EC 3.5.1.127 created 2017] |
|
|
|
|
EC |
3.5.1.128 |
Accepted name: |
deaminated glutathione amidase |
Reaction: |
N-(4-oxoglutaryl)-L-cysteinylglycine + H2O = 2-oxoglutarate + L-cysteinylglycine |
Glossary: |
N-(4-oxoglutaryl)-L-cysteinylglycine = deaminated glutathione |
Other name(s): |
dGSH deaminase; NIT1 (gene name) |
Systematic name: |
N-(4-oxoglutaryl)-L-cysteinylglycine amidohydrolase |
Comments: |
The enzyme, present in animals, fungi and bacteria, is involved in clearing cells of the toxic compound deaminated glutathione, which can be produced as an unwanted side product by several transaminases. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Peracchi, A., Veiga-da-Cunha, M., Kuhara, T., Ellens, K.W., Paczia, N., Stroobant, V., Seliga, A.K., Marlaire, S., Jaisson, S., Bommer, G.T., Sun, J., Huebner, K., Linster, C.L., Cooper, A.JL. and Van Schaftingen, E. Nit1 is a metabolite repair enzyme that hydrolyzes deaminated glutathione. Proc. Natl. Acad. Sci. USA 114 (2017) E3233–E3242. [DOI] [PMID: 28373563] |
|
[EC 3.5.1.128 created 2018] |
|
|
|
|
EC |
3.5.1.129 |
Accepted name: |
N5-(cytidine 5′-diphosphoramidyl)-L-glutamine hydrolase |
Reaction: |
N5-(cytidine 5′-diphosphoramidyl)-L-glutamine + H2O = cytidine 5′-diphosphoramidate + L-glutamate |
Other name(s): |
N5-(cytidine 5′-diphosphoramidyl)-L-glutamine deacylase |
Systematic name: |
N5-(cytidine 5′-diphosphoramidyl)-L-glutamine amidohydrolase |
Comments: |
The enzyme, characterized from the bacterium Campylobacter jejuni, is involved in formation of a unique O-methyl phosphoramidate modification on specific sugar residues within the bacterium’s capsular polysaccharides. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Taylor, Z.W., Brown, H.A., Holden, H.M. and Raushel, F.M. Biosynthesis of nucleoside diphosphoramidates in Campylobacter jejuni. Biochemistry 56 (2017) 6079–6082. [PMID: 29023101] |
|
[EC 3.5.1.129 created 2018] |
|
|
|
|
EC |
3.5.1.130 |
Accepted name: |
[amino group carrier protein]-lysine hydrolase |
Reaction: |
[amino group carrier protein]-C-terminal-γ-(L-lysyl)-L-glutamate + H2O = [amino group carrier protein]-C-terminal-L-glutamate + L-lysine |
Other name(s): |
lysK (gene name) |
Systematic name: |
[amino group carrier protein]-C-terminal-γ-L-lysyl-L-glutamate amidohydrolase |
Comments: |
The enzyme participates in an L-lysine biosynthetic pathway in certain species of archaea and bacteria. In some organisms the enzyme also catalyses the activity of EC 3.5.1.132, [amino group carrier protein]-ornithine hydrolase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Horie, A., Tomita, T., Saiki, A., Kono, H., Taka, H., Mineki, R., Fujimura, T., Nishiyama, C., Kuzuyama, T. and Nishiyama, M. Discovery of proteinaceous N-modification in lysine biosynthesis of Thermus thermophilus. Nat. Chem. Biol. 5 (2009) 673–679. [DOI] [PMID: 19620981] |
2. |
Ouchi, T., Tomita, T., Horie, A., Yoshida, A., Takahashi, K., Nishida, H., Lassak, K., Taka, H., Mineki, R., Fujimura, T., Kosono, S., Nishiyama, C., Masui, R., Kuramitsu, S., Albers, S.V., Kuzuyama, T. and Nishiyama, M. Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus. Nat. Chem. Biol. 9 (2013) 277–283. [DOI] [PMID: 23434852] |
3. |
Yoshida, A., Tomita, T., Atomi, H., Kuzuyama, T. and Nishiyama, M. Lysine biosynthesis of Thermococcus kodakarensis with the capacity to function as an ornithine biosynthetic system. J. Biol. Chem. 291 (2016) 21630–21643. [DOI] [PMID: 27566549] |
4. |
Fujita, S., Cho, S.H., Yoshida, A., Hasebe, F., Tomita, T., Kuzuyama, T. and Nishiyama, M. Crystal structure of LysK, an enzyme catalyzing the last step of lysine biosynthesis in Thermus thermophilus, in complex with lysine: Insight into the mechanism for recognition of the amino-group carrier protein, LysW. Biochem. Biophys. Res. Commun. 491 (2017) 409–415. [DOI] [PMID: 28720495] |
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[EC 3.5.1.130 created 2019] |
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EC |
3.5.1.131 |
Accepted name: |
1-carboxybiuret hydrolase |
Reaction: |
1-carboxybiuret + H2O = urea-1,3-dicarboxylate + NH3 |
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For diagram of atrazine catabolism, click here |
Glossary: |
carboxybiuret = carbamoylcarbamoylcarbamic acid |
Other name(s): |
atzEG (gene names) |
Systematic name: |
1-carboxybiuret amidohydrolase |
Comments: |
The enzyme, characterized from the bacterium Pseudomonas sp. ADP, participates in the degradation of cyanuric acid, an intermediate in the degradation of s-triazine herbicides such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine]. The enzyme is a heterotetramer composed of a catalytic subunit (AtzE) and an accessory subunit (AtzG) that stabilizes the complex. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Esquirol, L., Peat, T.S., Wilding, M., Liu, J.W., French, N.G., Hartley, C.J., Onagi, H., Nebl, T., Easton, C.J., Newman, J. and Scott, C. An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. J. Biol. Chem. 293 (2018) 7880–7891. [DOI] [PMID: 29523689] |
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[EC 3.5.1.131 created 2019] |
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EC |
3.5.1.132 |
Accepted name: |
[amino group carrier protein]-ornithine hydrolase |
Reaction: |
[amino group carrier protein]-C-terminal-γ-(L-ornithyl)-L-glutamate + H2O = [amino group carrier protein]-C-terminal-L-glutamate + L-ornithine |
Other name(s): |
lysK (gene name) |
Systematic name: |
[amino group carrier protein]-C-terminal-γ-L-ornithyl-L-glutamate amidohydrolase |
Comments: |
The enzyme participates in an L-arginine biosynthetic pathways in certain species of archaea and bacteria. In all cases known so far the enzyme also catalyses the activity of EC 3.5.1.130, [amino group carrier protein]-lysine hydrolase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Ouchi, T., Tomita, T., Horie, A., Yoshida, A., Takahashi, K., Nishida, H., Lassak, K., Taka, H., Mineki, R., Fujimura, T., Kosono, S., Nishiyama, C., Masui, R., Kuramitsu, S., Albers, S.V., Kuzuyama, T. and Nishiyama, M. Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus. Nat. Chem. Biol. 9 (2013) 277–283. [DOI] [PMID: 23434852] |
2. |
Yoshida, A., Tomita, T., Atomi, H., Kuzuyama, T. and Nishiyama, M. Lysine biosynthesis of Thermococcus kodakarensis with the capacity to function as an ornithine biosynthetic system. J. Biol. Chem. 291 (2016) 21630–21643. [DOI] [PMID: 27566549] |
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[EC 3.5.1.132 created 2019] |
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EC |
3.5.1.133 |
Accepted name: |
Nα-acyl-L-glutamine aminoacylase |
Reaction: |
an Nα-acyl-L-glutamine + H2O = L-glutamine + a carboxylate |
Other name(s): |
agaA (gene name); axillary malodor releasing enzyme; AMRE |
Systematic name: |
Nα-acyl-L-glutamine amidohydrolase (carboxylate-forming) |
Comments: |
Requires Zn2+. The enzyme, characterized from the bacterium Corynebacterium sp. Ax20, hydrolyses odorless Nα-acyl-L-glutamine conjugates of short- and medium-chain fatty acids, releasing axillary malodor compounds. While the enzyme is highly specific for the L-glutamine moiety, it is quite promiscuous regarding the acyl moiety. The two most common products of the enzyme’s activity in axillary secretions are (2E)-3-methylhex-2-enoate and 3-hydroxy-3-methylhexanoate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Natsch, A., Gfeller, H., Gygax, P., Schmid, J. and Acuna, G. A specific bacterial aminoacylase cleaves odorant precursors secreted in the human axilla. J. Biol. Chem. 278 (2003) 5718–5727. [PMID: 12468539] |
2. |
Natsch, A., Gfeller, H., Gygax, P. and Schmid, J. Isolation of a bacterial enzyme releasing axillary malodor and its use as a screening target for novel deodorant formulations. Int J Cosmet Sci 27 (2005) 115–122. [PMID: 18492161] |
3. |
Natsch, A., Derrer, S., Flachsmann, F. and Schmid, J. A broad diversity of volatile carboxylic acids, released by a bacterial aminoacylase from axilla secretions, as candidate molecules for the determination of human-body odor type. Chem. Biodivers. 3 (2006) 1–20. [PMID: 17193210] |
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[EC 3.5.1.133 created 2019] |
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EC |
3.5.1.134 |
Accepted name: |
(indol-3-yl)acetyl-L-aspartate hydrolase |
Reaction: |
(indol-3-yl)acetyl-L-aspartate + H2O = (indol-3-yl)acetate + L-aspartate |
Other name(s): |
indole-3-acetyl-L-aspartate hydrolase; iaaspH (gene name) |
Systematic name: |
(indol-3-yl)acetyl-L-aspartate amidohydrolase |
Comments: |
The enzyme, isolated from the bacterium Pantoea agglomerans, is specific for its substrate and does not act efficiently on other indole-3-acetate conjugates. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Chou, J.C., Kuleck, G.A., Cohen, J.D. and Mulbry, W.W. Partial purification and characterization of an inducible indole-3-acetyl-L-aspartic acid hydrolase from enterobacter agglomerans. Plant Physiol. 112 (1996) 1281–1287. [PMID: 12226446] |
2. |
Chou, J.C., Mulbry, W.W. and Cohen, J.D. The gene for indole-3-acetyl-L-aspartic acid hydrolase from Enterobacter agglomerans: molecular cloning, nucleotide sequence, and expression in Escherichia coli. Mol. Gen. Genet. 259 (1998) 172–178. [PMID: 9747708] |
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[EC 3.5.1.134 created 2019] |
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EC |
3.5.1.135 |
Accepted name: |
N4-acetylcytidine amidohydrolase |
Reaction: |
N4-acetylcytidine + H2O = cytidine + acetate |
Other name(s): |
yqfB (gene name) |
Systematic name: |
N4-acetylcytidine amidohydrolase |
Comments: |
The enzyme from the bacterium Escherichia coli is one of the smallest known monomeric amidohydrolases (103-amino acids). The enzyme is active towards a wide range of N4-acylcytosines/cytidines, but is by far most active against N4-acetylcytidine. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Shen, Y., Atreya, H.S., Liu, G. and Szyperski, T. G-matrix Fourier transform NOESY-based protocol for high-quality protein structure determination. J. Am. Chem. Soc. 127 (2005) 9085–9099. [PMID: 15969587] |
2. |
Stanislauskiene, R., Laurynenas, A., Rutkiene, R., Aucynaite, A., Tauraite, D., Meskiene, R., Urbeliene, N., Kaupinis, A., Valius, M., Kaliniene, L. and Meskys, R. YqfB protein from Escherichia coli: an atypical amidohydrolase active towards N4-acylcytosine derivatives. Sci. Rep. 10:788 (2020). [PMID: 31964920] |
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[EC 3.5.1.135 created 2020] |
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EC |
3.5.1.136 |
Accepted name: |
N,N′-diacetylchitobiose non-reducing end deacetylase |
Reaction: |
N,N′-diacetylchitobiose + H2O = β-D-glucosaminyl-(1→4)-N-acetyl-D-glucosamine + acetate |
Other name(s): |
diacetylchitobiose deacetylase (ambiguous); cda (gene name) |
Systematic name: |
N,N′-diacetylchitobiose non-reducing end acetylhydrolase |
Comments: |
The enzyme, characterized from the archaeons Thermococcus kodakarensis and Pyrococcus horikoshii, deacetylates the non-reducing residue of N,N′-diacetylchitobiose, the end product of the archaeal chitinase, to produce β-D-glucosaminyl-(1→4)-N-acetyl-D-glucosamine. This is in contrast to EC 3.5.1.105, chitin disaccharide deacetylase, which deacetylates N,N′-diacetylchitobiose at the reducing residue to produce N-acetyl-β-D-glucosaminyl-(1→4)-D-glucosamine. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Tanaka, T., Fukui, T., Fujiwara, S., Atomi, H. and Imanaka, T. Concerted action of diacetylchitobiose deacetylase and exo-β-D-glucosaminidase in a novel chitinolytic pathway in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J. Biol. Chem. 279 (2004) 30021–30027. [DOI] [PMID: 15136574] |
2. |
Mine, S., Ikegami, T., Kawasaki, K., Nakamura, T. and Uegaki, K. Expression, refolding, and purification of active diacetylchitobiose deacetylase from Pyrococcus horikoshii. Protein Expr. Purif. 84 (2012) 265–269. [DOI] [PMID: 22713621] |
3. |
Nakamura, T., Yonezawa, Y., Tsuchiya, Y., Niiyama, M., Ida, K., Oshima, M., Morita, J. and Uegaki, K. Substrate recognition of N,N′-diacetylchitobiose deacetylase from Pyrococcus horikoshii. J. Struct. Biol. 195:S1047-8477( (2016). [DOI] [PMID: 27456364] |
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[EC 3.5.1.136 created 2020] |
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EC |
3.5.1.137 |
Accepted name: |
N-methylcarbamate hydrolase |
Reaction: |
an N-methyl carbamate ester + H2O = an alcohol + methylamine + CO2 |
Glossary: |
carbaryl = N-methyl-1-naphthyl carbamate |
Other name(s): |
mcbA (gene name); cehA (gene name); cfdJ (gene name); carbaryl hydrolase; carbofuran hydrolase |
Systematic name: |
N-methyl carbamate ester hydrolase |
Comments: |
The enzyme catalyses the first step in the degradation of several carbamate insecticides such as carbaryl, carbofuran, isoprocarb, propoxur, aldicarb and oxamyl. It catalyses the cleavage of the ester bond to release N-methylcarbamate, which spontaneously hydrolyses to methylamine and CO2. The enzymes from several Gram-negative bacteria were shown to be located in the periplasm. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Mulbry, W.W. and Eaton, R.W. Purification and characterization of the N-methylcarbamate hydrolase from Pseudomonas strain CRL-OK. Appl. Environ. Microbiol. 57 (1991) 3679–3682. [PMID: 1785941] |
2. |
Hayatsu, M. and Nagata, T. Purification and characterization of carbaryl hydrolase from Blastobacter sp. strain M501. Appl. Environ. Microbiol. 59 (1993) 2121–2125. [PMID: 16348989] |
3. |
Chapalmadugu, S. and Chaudhry, G.R. Isolation of a constitutively expressed enzyme for hydrolysis of carbaryl in Pseudomonas aeruginosa. J. Bacteriol. 175 (1993) 6711–6716. [DOI] [PMID: 8407847] |
4. |
Hayatsu, M., Mizutani, A., Hashimoto, M., Sato, K. and Hayano, K. Purification and characterization of carbaryl hydrolase from Arthrobacter sp. RC100. FEMS Microbiol. Lett. 201 (2001) 99–103. [DOI] [PMID: 11445174] |
5. |
Hashimoto, M., Fukui, M., Hayano, K. and Hayatsu, M. Nucleotide sequence and genetic structure of a novel carbaryl hydrolase gene (cehA) from Rhizobium sp. strain AC100. Appl. Environ. Microbiol. 68 (2002) 1220–1227. [DOI] [PMID: 11872471] |
6. |
Zhang, Q., Liu, Y. and Liu, Y.H. Purification and characterization of a novel carbaryl hydrolase from Aspergillus niger PY168. FEMS Microbiol. Lett. 228 (2003) 39–44. [DOI] [PMID: 14612234] |
7. |
Ozturk, B., Ghequire, M., Nguyen, T.P., De Mot, R., Wattiez, R. and Springael, D. Expanded insecticide catabolic activity gained by a single nucleotide substitution in a bacterial carbamate hydrolase gene. Environ. Microbiol. 18 (2016) 4878–4887. [DOI] [PMID: 27312345] |
8. |
Kamini, Shetty, D., Trivedi, V.D., Varunjikar, M. and Phale, P.S. Compartmentalization of the carbaryl degradation pathway: molecular characterization of inducible periplasmic carbaryl hydrolase from Pseudomonas spp. Appl. Environ. Microbiol. 84:e02115-17 (2018). [DOI] [PMID: 29079626] |
9. |
Yan, X., Jin, W., Wu, G., Jiang, W., Yang, Z., Ji, J., Qiu, J., He, J., Jiang, J. and Hong, Q. Hydrolase CehA and monooxygenase CfdC are responsible for carbofuran degradation in Sphingomonas sp. strain CDS-1. Appl. Environ. Microbiol. 84 (2018) . [DOI] [PMID: 29884759] |
10. |
Jiang, W., Gao, Q., Zhang, L., Wang, H., Zhang, M., Liu, X., Zhou, Y., Ke, Z., Wu, C., Qiu, J. and Hong, Q. Identification of the key amino acid sites of the carbofuran hydrolase CehA from a newly isolated carbofuran-degrading strain Sphingbium sp. CFD-1. Ecotoxicol Environ Saf 189:109938 (2020). [DOI] [PMID: 31759739] |
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[EC 3.5.1.137 created 2021] |
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EC |
3.5.1.138 |
Accepted name: |
lipoamidase |
Reaction: |
a [lipoyl-carrier protein]-N6-[(R)-lipoyl]-L-lysine + H2O = a [lipoyl-carrier protein]-L-lysine + (R)-lipoate |
Other name(s): |
pyruvate dehydrogenase inactivase |
Systematic name: |
[lipoyl-carrier protein]-N6-[(R)-lipoyl]-L-lysine amidohydrolase |
Comments: |
The enzyme, characterized from the bacterium Enterococcus faecalis, is a member of the Ser-Ser-Lys triad amidohydrolase family. cf. EC 2.3.1.313, NAD-dependent lipoamidase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Reed, L.J., Koike, M., Levitch, M.E., Leach, F.R. Studies on the nature and reactions of protein-bound lipoic acid. J. Biol. Chem. 232 (1958) 143–158. [DOI] [PMID: 13549405] |
2. |
Suzuki, K, Reed L.J. Lipoamidase. J. Biol. Chem. 238 (1963) 4021–4025. [DOI] [PMID: 14086741] |
3. |
Jiang, Y. and Cronan, J.E. Expression cloning and demonstration of Enterococcus faecalis lipoamidase (pyruvate dehydrogenase inactivase) as a Ser-Ser-Lys triad amidohydrolase. J. Biol. Chem. 280 (2005) 2244–2256. [DOI] [PMID: 15528186] |
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[EC 3.5.1.138 created 2023] |
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