| EC |
2.3.3.17 |
| Accepted name: |
methylthioalkylmalate synthase |
| Reaction: |
an ω-(methylsulfanyl)-2-oxoalkanoate + acetyl-CoA + H2O = a 2-[ω-(methylsulfanyl)alkyl]malate + CoA |
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For diagram of L-Homomethionine biosynthesis, click here |
| Other name(s): |
MAM1 (gene name); MAM3 (gene name); acetyl-CoA:ω-(methylthio)-2-oxoalkanoate C-acetyltransferase |
| Systematic name: |
acetyl-CoA:ω-(methylsulfanyl)-2-oxoalkanoate C-acetyltransferase |
| 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. Two forms are known - MAM1 catalyses only only the first two rounds of methionine chain elongation, while MAM3 catalyses all six cycles, up to formation of L-hexahomomethionine. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Textor, S., Bartram, S., Kroymann, J., Falk, K.L., Hick, A., Pickett, J.A. and Gershenzon, J. Biosynthesis of methionine-derived glucosinolates in Arabidopsis thaliana: recombinant expression and characterization of methylthioalkylmalate synthase, the condensing enzyme of the chain-elongation cycle. Planta 218 (2004) 1026–1035. [DOI] [PMID: 14740211] |
| 2. |
Textor, S., de Kraker, J.W., Hause, B., Gershenzon, J. and Tokuhisa, J.G. MAM3 catalyzes the formation of all aliphatic glucosinolate chain lengths in Arabidopsis. Plant Physiol. 144 (2007) 60–71. [DOI] [PMID: 17369439] |
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| [EC 2.3.3.17 created 2016] |
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