The Enzyme Database

Your query returned 11 entries.    printer_iconPrintable version



EC 3.5.1.6     
Accepted name: β-ureidopropionase
Reaction: 3-ureidopropanoate + H2O = β-alanine + CO2 + NH3
For diagram of pyrimidine catabolism, click here
Glossary: 3-ureidopropanoate = N-carbamoyl-β-alanine
Other name(s): N-carbamoyl-β-alanine amidohydrolase
Systematic name: 3-ureidopropanoate amidohydrolase
Comments: The animal enzyme also acts on β-ureidoisobutyrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9027-27-4
References:
1.  Campbell, L.L. Reductive degradation of pyrimidines. 5. Enzymatic conversion of N-carbamyl-β-alanine to β-alanine, carbon dioxide, and ammonia. J. Biol. Chem. 235 (1960) 2375–2378. [PMID: 13849303]
2.  Caravaca, J. and Grisolia, S. Enzymatic decarbamylation of carbamyl β-alanine and carbamyl β-aminoisobutyric acid. J. Biol. Chem. 231 (1958) 357–365. [PMID: 13538975]
3.  Traut, T.W. and Loechel, S. Pyrimidine catabolism: individual characterization of the three sequential enzymes with a new assay. Biochemistry 23 (1984) 2533–2539. [PMID: 6433973]
[EC 3.5.1.6 created 1961]
 
 
EC 3.5.1.60     
Accepted name: N-(long-chain-acyl)ethanolamine deacylase
Reaction: N-(long-chain-acyl)ethanolamine + H2O = a long-chain carboxylate + ethanolamine
Other name(s): N-acylethanolamine amidohydrolase; acylethanolamine amidase
Systematic name: N-(long-chain-acyl)ethanolamine amidohydrolase
Comments: Does not act on N-acylsphingosine or N,O-diacylethanolamine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 99283-61-1
References:
1.  Schmid, P.C., Zuzarte-Augustin, M.L. and Schmid, H.H.O. Properties of rat liver N-acylethanolamine amidohydrolase. J. Biol. Chem. 260 (1985) 14145–14149. [PMID: 4055775]
[EC 3.5.1.60 created 1989]
 
 
EC 3.5.1.61     
Accepted name: mimosinase
Reaction: (S)-2-amino-3-(3-hydroxy-4-oxo-4H-pyridin-1-yl)propanoate + H2O = 3-hydroxy-4H-pyrid-4-one + L-serine
Systematic name: mimosine amidohydrolase
Comments: An enzyme from Leucaena leucocephala leaf, which also contains the toxic amino acid, mimosine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 104118-49-2
References:
1.  Tangendjaja, B., Lowry, J.B. and Wills, R.H. Isolation of a mimosine degrading enzyme from Leucaena leaf. J. Sci. Food Agric. 37 (1986) 523–526.
[EC 3.5.1.61 created 1989]
 
 
EC 3.5.1.62     
Accepted name: acetylputrescine deacetylase
Reaction: N-acetylputrescine + H2O = acetate + putrescine
Glossary: putrescine = butane-1,4-diamine
spermidine = N-(3-aminopropyl)butane-1,4-diamine
Systematic name: N-acetylputrescine acetylhydrolase
Comments: The enzyme from Micrococcus luteus also acts on N8-acetylspermidine and acetylcadaverine, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 103679-48-7
References:
1.  Suzuki, O., Ishikawa, Y., Miyazaki, K., Izu, K. and Matsumoto, T. Acetylputrescine deacetylase from Micrococcus luteus K-11. Biochim. Biophys. Acta 882 (1986) 140–142.
[EC 3.5.1.62 created 1989]
 
 
EC 3.5.1.63     
Accepted name: 4-acetamidobutyrate deacetylase
Reaction: 4-acetamidobutanoate + H2O = acetate + 4-aminobutanoate
Glossary: 4-aminobutanoate = γ-aminobutyrate = GABA
Systematic name: 4-acetamidobutanoate amidohydrolase
Comments: Also acts on N-acetyl-β-alanine and 5-acetamidopentanoate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 102347-82-0
References:
1.  Haywood, G.W. and Large, P.J. 4-Acetamidobutyrate deacetylase in the yeast Candida boidinii grown on putrescine or spermidine as sole nitrogen source and its probable role in polyamine catabolism. J. Gen. Microbiol. 132 (1986) 7–14.
[EC 3.5.1.63 created 1989]
 
 
EC 3.5.1.64     
Accepted name: Nα-benzyloxycarbonylleucine hydrolase
Reaction: Nα-benzyloxycarbonyl-L-leucine + H2O = benzyl alcohol + CO2 + L-leucine
Other name(s): benzyloxycarbonylleucine hydrolase; Nα-benzyloxycarbonyl amino acid urethane hydrolase IV; α-N-benzyloxycarbonyl-L-leucine urethanehydrolase
Systematic name: Nα-benzyloxycarbonyl-L-leucine urethanehydrolase
Comments: Also acts on Nα-t-butoxycarbonyl-L-leucine, and, more slowly, on the corresponding derivatives of L-aspartate, L-methionine, L-glutamate and L-alanine. cf. EC 3.5.1.58 N-benzyloxycarbonylglycine hydrolase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 100630-47-5
References:
1.  Matsumura, E., Shin, T., Murao, S., Sakaguchi, M. and Kawano, T. A novel enzyme, Nα-benzyloxycarbonyl amino acid urethane hydrolase IV. Agric. Biol. Chem. 49 (1985) 3643–3645.
[EC 3.5.1.64 created 1989]
 
 
EC 3.5.1.65     
Accepted name: theanine hydrolase
Reaction: N5-ethyl-L-glutamine + H2O = L-glutamate + ethylamine
Glossary: L-theanine = N5-ethyl-L-glutamine
Other name(s): L-theanine amidohydrolase; 5-N-ethyl-L-glutamine amidohydrolase
Systematic name: N5-ethyl-L-glutamine amidohydrolase
Comments: Also acts on other N-alkyl-L-glutamines.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 99533-51-4
References:
1.  Tsushida, T. and Takeo, T. An enzyme hydrolyzing L-theanine in tea leaves. Agric. Biol. Chem. 49 (1985) 2913–2917.
[EC 3.5.1.65 created 1989]
 
 
EC 3.5.1.66     
Accepted name: 2-(hydroxymethyl)-3-(acetamidomethylene)succinate hydrolase
Reaction: 2-(hydroxymethyl)-3-(acetamidomethylene)succinate + 2 H2O = acetate + 2-(hydroxymethyl)-4-oxobutanoate + NH3 + CO2
Other name(s): compound B hydrolase; α-hydroxymethyl-α’-(N-acetylaminomethylene)succinic acid hydrolase
Systematic name: 2-(hydroxymethyl)-3-(acetamidomethylene)succinate amidohydrolase (deaminating, decarboxylating)
Comments: Involved in the degradation of pyridoxin by Pseudomonas and Arthrobacter.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 95829-26-8
References:
1.  Huynh, M.S. and Snell, E.E. Enzymes of vitamin B6 degradation. Purification and properties of two N-acetylamidohydrolases. J. Biol. Chem. 260 (1985) 2379–2383. [PMID: 3972793]
[EC 3.5.1.66 created 1989]
 
 
EC 3.5.1.67     
Accepted name: 4-methyleneglutaminase
Reaction: 4-methylene-L-glutamine + H2O = 4-methylene-L-glutamate + NH3
Other name(s): 4-methyleneglutamine deamidase; 4-methyleneglutamine amidohydrolase
Systematic name: 4-methylene-L-glutamine amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 86855-36-9
References:
1.  Ibrahim, S.A., Lea, P.J. and Fowden, L. Preparation and properties of 4-methyleneglutaminase from the leaves of peanut (Arachis hypogaea). Phytochemistry 23 (1984) 1545–1549.
[EC 3.5.1.67 created 1989]
 
 
EC 3.5.1.68     
Accepted name: N-formylglutamate deformylase
Reaction: N-formyl-L-glutamate + H2O = formate + L-glutamate
For diagram of histidine catabolism, click here
Other name(s): β-citryl-L-glutamate hydrolase; formylglutamate deformylase; N-formylglutamate hydrolase; β-citrylglutamate amidase; β-citryl-L-glutamate amidohydrolase; β-citryl-L-glutamate amidase; β-citryl-L-glutamate-hydrolyzing enzyme
Systematic name: N-formyl-L-glutamate amidohydrolase
Comments: The animal enzyme also acts on β-citryl-L-glutamate and β-citryl-L-glutamine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 97286-12-9
References:
1.  Hu, L., Mulfinger, L.M. and Phillips, A.T. Purification and properties of formylglutamate amidohydrolase from Pseudomonas putida. J. Bacteriol. 169 (1987) 4696–4702. [DOI] [PMID: 3308850]
2.  Miyake, M., Innami, T. and Kakimoto, Y. A β-citryl-L-glutamate-hydrolysing enzyme in rat testes. Biochim. Biophys. Acta 760 (1983) 206–214. [DOI] [PMID: 6414521]
[EC 3.5.1.68 created 1989]
 
 
EC 3.5.1.69     
Accepted name: glycosphingolipid deacylase
Reaction: Hydrolysis of gangliosides and neutral glycosphingolipids, releasing fatty acids to form the lyso-derivatives
Other name(s): glycosphingolipid ceramide deacylase
Systematic name: glycosphingolipid amidohydrolase
Comments: Does not act on sphingolipids such as ceramide. Not identical with EC 3.5.1.23 ceramidase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 122544-53-0
References:
1.  Hirabayashi, Y., Kimura, M., Matsumoto, M., Yamamoto, K., Kadowaki, S. and Tochikura, T. A novel glycosphingolipid hydrolyzing enzyme, glycosphingolipid ceramide deacylase, which cleaves the linkage between the fatty acid and sphingosine base in glycosphingolipids. J. Biochem. (Tokyo) 103 (1988) 1–4. [PMID: 3360750]
[EC 3.5.1.69 created 1990]
 
 


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