The Enzyme Database

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Accepted name: 2-(ω-methylthio)alkylmalate dehydratase
Reaction: (1) a 2-[(ω-methylsulfanyl)alkyl]malate = a 2-[(ω-methylsulfanyl)alkyl]maleate + H2O
(2) a 3-[(ω-methylsulfanyl)alkyl]malate = a 2-[(ω-methylsulfanyl)alkyl]maleate + H2O
For diagram of L-Homomethionine biosynthesis, click here
Other name(s): IPMI (gene name); 2-[(ω-methylthio)alkyl]malate hydro-lyase (2-[(ω-methylthio)alkyl]maleate-forming)
Systematic name: 2-[(ω-methylsulfanyl)alkyl]malate hydro-lyase (2-[(ω-methylsulfanyl)alkyl]maleate-forming)
Comments: The enzyme, characterized from the plant Arabidopsis thaliana, is involved in the L-methionine side-chain elongation pathway, forming substrates for the biosynthesis of aliphatic glucosinolates. By catalysing a dehydration of a 2-[(ω-methylsulfanyl)alkyl]maleate, followed by a hydration at a different position, the enzyme achieves the isomerization of its substrates. The enzyme is a heterodimer comprising a large and a small subunits. The large subunit can also bind to an alternative small subunit, forming EC, 3-isopropylmalate dehydratase, which participates in L-leucine biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Knill, T., Reichelt, M., Paetz, C., Gershenzon, J. and Binder, S. Arabidopsis thaliana encodes a bacterial-type heterodimeric isopropylmalate isomerase involved in both Leu biosynthesis and the Met chain elongation pathway of glucosinolate formation. Plant Mol. Biol. 71 (2009) 227–239. [DOI] [PMID: 19597944]
[EC created 2016]

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