Biology:3-chloro-D-alanine dehydrochlorinase
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Short description: Class of enzymes
3-chloro-D-alanine dehydrochlorinase | |||||||||
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Identifiers | |||||||||
EC number | 4.5.1.2 | ||||||||
CAS number | 78990-65-5 | ||||||||
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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The enzyme 3-chloro-D-alanine dehydrochlorinase (EC 4.5.1.2) catalyzes the reaction
- 3-chloro-D-alanine + H2O = pyruvate + chloride + NH3 (overall reaction)
- (1a) 3-chloro-D-alanine = chloride + 2-aminoprop-2-enoate
- (1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
- (1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous)
This enzyme belongs to the family of lyases, specifically the class of carbon-halide lyases. The systematic name of this enzyme class is 3-chloro-D-alanine chloride-lyase (deaminating; pyruvate-forming). Other names in common use include β-chloro-D-alanine dehydrochlorinase, and 3-chloro-D-alanine chloride-lyase (deaminating). It employs one cofactor, pyridoxal phosphate.
References
- "Physiological comparison of D-cysteine desulfhydrase of Escherichia coli with 3-chloro-D-alanine dehydrochlorinase of Pseudomonas putida CR 1-1". Archives of Microbiology 149 (5): 413–6. 1988. doi:10.1007/BF00425580. PMID 3132906.
- "Synthesis of D-cysteine from 3-chloro-D-alanine and hydrogen sulfide by 3-chloro-D-alanine hydrogen chloride-lyase (deaminating) of Pseudomonas putida". Biochemical and Biophysical Research Communications 100 (3): 1104–10. June 1981. doi:10.1016/0006-291X(81)91937-9. PMID 6791643.
Original source: https://en.wikipedia.org/wiki/3-chloro-D-alanine dehydrochlorinase.
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