The Enzyme Database

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EC 4.2.1.166     
Accepted name: phosphinomethylmalate isomerase
Reaction: 2-(hydroxyphosphonoylmethyl)malate = 3-(hydroxyphosphonoylmethyl)malate (overall reaction)
(1a) 2-(hydroxyphosphonoylmethyl)malate = 2-(phosphinatomethylidene)butanedioate + H2O
(1b) 2-(phosphinatomethylidene)butanedioate + H2O = 3-(hydroxyphosphonoylmethyl)malate
Glossary: 2-(hydroxyphosphonoylmethyl)malate = 2-hydroxy-2-(hydroxyphosphonoylmethyl)butanedioate
3-(hydroxyphosphonoylmethyl)malate = 2-hydroxy-3-(hydroxyphosphonoylmethyl)butanedioate
Other name(s): pmi (gene name)
Systematic name: 2-(phosphinomethyl)malate hydro-lyase [3-(phosphinomethyl)malate-forming]
Comments: The enzyme, characterized from the bacterium Streptomyces viridochromogenes, is involved in bialaphos biosynthesis. The enzyme from the bacterium Kitasatospora phosalacinea participates in the biosynthesis of the related compound phosalacine. Both compounds contain the nonproteinogenic amino acid L-phosphinothricin that acts as a potent inhibitor of EC 6.3.1.2, glutamine synthetase. The similar enzyme EC 4.2.1.3, aconitate hydratase, cannot catalyse this reaction.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Heinzelmann, E., Kienzlen, G., Kaspar, S., Recktenwald, J., Wohlleben, W. and Schwartz, D. The phosphinomethylmalate isomerase gene pmi, encoding an aconitase-like enzyme, is involved in the synthesis of phosphinothricin tripeptide in Streptomyces viridochromogenes. Appl. Environ. Microbiol. 67 (2001) 3603–3609. [PMID: 11472937]
[EC 4.2.1.166 created 2016]
 
 


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