EC - 3-chloro-D-alanine dehydrochlorinase

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IntEnz Enzyme Nomenclature


Accepted name:
3-chloro-D-alanine dehydrochlorinase
Other names:
β-chloro-D-alanine dehydrochlorinase
3-chloro-D-alanine chloride-lyase (deaminating)
Systematic name:
3-chloro-D-alanine chloride-lyase (deaminating; pyruvate-forming)




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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0019149
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 : 413-416 (1988). [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 : 1104-1110 (1981). [PMID: 6791643]

[EC created 1984]