3-aminobutyryl-CoA ammonia-lyase
The enzyme 3-aminobutyryl-CoA ammonia-lyase (EC 4.3.1.14) catalyzes the chemical reaction
- L-3-aminobutyryl-CoA crotonoyl-CoA + NH3
3-aminobutyryl-CoA ammonia-lyase | |||||||||
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Identifiers | |||||||||
EC no. | 4.3.1.14 | ||||||||
CAS no. | 55467-41-9 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is L-3-aminobutyryl-CoA ammonia-lyase (crotonoyl-CoA-forming). Other names in common use include L-3-aminobutyryl-CoA deaminase, and L-3-aminobutyryl-CoA ammonia-lyase.
References
- Jeng I, Barker HA (October 1974). "Purification and properties of l-3-aminobutyryl coenzyme A deaminase from a lysine-fermenting Clostridium". The Journal of Biological Chemistry. 249 (20): 6578–84. PMID 4420467.
- Barker HA, Kahn JM, Chew S (September 1980). "Enzymes involved in 3,5-diaminohexanoate degradation by Brevibacterium sp". Journal of Bacteriology. 143 (3): 1165–70. PMC 294469. PMID 7410315.
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