The Enzyme Database

Your query returned 2 entries.    printer_iconPrintable version



EC 2.3.1.247     
Accepted name: 3-keto-5-aminohexanoate cleavage enzyme
Reaction: (5S)-5-amino-3-oxohexanoate + acetyl-CoA = L-3-aminobutanoyl-CoA + acetoacetate
For diagram of lysine catabolism, click here
Glossary: L-3-aminobutyryl-CoA = (3S)-3-aminobutanoyl-CoA
Other name(s): kce (gene name)
Systematic name: (5S)-5-amino-3-oxohexanoate:acetyl-CoA ethylamine transferase
Comments: Requires Zn2+. The enzyme, isolated from the bacteria Fusobacterium nucleatum and Cloacimonas acidaminovorans, is involved in the anaerobic fermentation of lysine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Barker, H.A., Kahn, J.M. and Hedrick, L. Pathway of lysine degradation in Fusobacterium nucleatum. J. Bacteriol. 152 (1982) 201–207. [PMID: 6811551]
2.  Kreimeyer, A., Perret, A., Lechaplais, C., Vallenet, D., Medigue, C., Salanoubat, M. and Weissenbach, J. Identification of the last unknown genes in the fermentation pathway of lysine. J. Biol. Chem. 282 (2007) 7191–7197. [DOI] [PMID: 17166837]
3.  Bellinzoni, M., Bastard, K., Perret, A., Zaparucha, A., Perchat, N., Vergne, C., Wagner, T., de Melo-Minardi, R.C., Artiguenave, F., Cohen, G.N., Weissenbach, J., Salanoubat, M. and Alzari, P.M. 3-Keto-5-aminohexanoate cleavage enzyme: a common fold for an uncommon Claisen-type condensation. J. Biol. Chem. 286 (2011) 27399–27405. [DOI] [PMID: 21632536]
[EC 2.3.1.247 created 2015]
 
 
EC 4.3.1.14     
Accepted name: 3-aminobutyryl-CoA ammonia-lyase
Reaction: L-3-aminobutyryl-CoA = crotonoyl-CoA + NH3
For diagram of lysine catabolism, click here
Other name(s): L-3-aminobutyryl-CoA deaminase; L-3-aminobutyryl-CoA ammonia-lyase
Systematic name: L-3-aminobutyryl-CoA ammonia-lyase (crotonoyl-CoA-forming)
Comments: Hydroxylamine can replace ammonia as a substrate. Crotonoyl-pantetheine can replace crotonoyl-CoA but it is a poorer substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 55467-41-9
References:
1.  Jeng, I.-M., Barker, H.A. Purification and properties of L-3-aminobutyryl coenzyme A deaminase from a lysine-fermenting Clostridium. J. Biol. Chem. 249 (1974) 6578–6584. [PMID: 4420467]
2.  Barker, H.A., Kahn, J.M., Chew, S. Enzymes involved in 3,5-diaminohexanoate degradation by Brevibacterium sp. J. Bacteriol. 143 (1980) 1165–1170. [PMID: 7410315]
[EC 4.3.1.14 created 1999]
 
 


Data © 2001–2020 IUBMB
Web site © 2005–2020 Andrew McDonald