The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: 3-chloro-D-alanine dehydrochlorinase
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)
Other name(s): β-chloro-D-alanine dehydrochlorinase; 3-chloro-D-alanine chloride-lyase (deaminating)
Systematic name: 3-chloro-D-alanine chloride-lyase (deaminating; pyruvate-forming)
Comments: A pyridoxal-phosphate protein. The enzyme cleaves a carbon-chlorine bond, releasing a chloride and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC, 2-iminobutanoate/2-iminopropanoate deaminase. The enzyme’s activity can also result in β-replacement reactions, e.g. in the presence of hydrogen sulfide it can convert 3-chloro-D-alanine into D-cysteine and chloride.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 78990-65-5
1.  Nagasawa, T., Ishii, T. and Yamada, H. Physiological comparison of D-cysteine desulfhydrase of Escherichia coli with 3-chloro-D-alanine dehydrochlorinase of Pseudomonas putida CR 1-1. Arch. Microbiol. 149 (1988) 413–416. [PMID: 3132906]
2.  Yamada, H., Nagasawa, T., Ohkishi, H., Kawakami, B. and Tani, Y. Synthesis of D-cysteine from 3-chloro-D-alanine and hydrogen sulfide by 3-chloro-D-alanine hydrogen chloride-lyase (deaminating) of Pseudomonas putida. Biochem. Biophys. Res. Commun. 100 (1981) 1104–1110. [DOI] [PMID: 6791643]
[EC created 1984]

Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald