KEGG   ENZYME: 2.3.3.17Help
Entry
EC 2.3.3.17                 Enzyme                                 

Name
methylthioalkylmalate synthase;
MAM1 (gene name);
MAM3 (gene name);
acetyl-CoA:omega-(methylthio)-2-oxoalkanoate C-acetyltransferase
Class
Transferases;
Acyltransferases;
Acyl groups converted into alkyl groups on transfer
BRITE hierarchy
Sysname
acetyl-CoA:omega-(methylsulfanyl)-2-oxoalkanoate C-acetyltransferase
Reaction(IUBMB)
an omega-(methylsulfanyl)-2-oxoalkanoate + acetyl-CoA + H2O = a 2-[omega-(methylsulfanyl)alkyl]malate + CoA
Reaction(KEGG)
Substrate
omega-(methylsulfanyl)-2-oxoalkanoate;
acetyl-CoA [CPD:C00024];
H2O [CPD:C00001]
Product
2-[omega-(methylsulfanyl)alkyl]malate;
CoA [CPD:C00010]
Comment
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.
History
EC 2.3.3.17 created 2016
Pathway
ec00966  Glucosinolate biosynthesis
ec01110  Biosynthesis of secondary metabolites
Orthology
K15741  methylthioalkylmalate synthase 1
K15742  methylthioalkylmalate synthase 3
Genes
ATH: AT5G23010(MAM1) AT5G23020(IMS2)
ALY: ARALYDRAFT_910306 ARALYDRAFT_910307
CRB: 17883723 17883860
CSAT: 104770650
EUS: EUTSA_v10004072mg EUTSA_v10005522mg
BRP: 103853322(MAM1-2) 103854915(GSL-Elong) 103860537(MAM3-1) 103860538(MAM1-1) 103861112 103868184
BNA: 106377269 106434598
BOE: 106301761 106324637 106325524
Taxonomy
Reference
1  [PMID:14740211]
  Authors
Textor S, Bartram S, Kroymann J, Falk KL, Hick A, Pickett JA, Gershenzon J.
  Title
Biosynthesis of methionine-derived glucosinolates in Arabidopsis thaliana: recombinant expression and characterization of methylthioalkylmalate synthase, the condensing enzyme of the chain-elongation cycle.
  Journal
Planta 218:1026-35 (2004)
DOI:10.1007/s00425-003-1184-3
  Sequence
[ath:AT5G23010]
Reference
2  [PMID:17369439]
  Authors
Textor S, de Kraker JW, Hause B, Gershenzon J, Tokuhisa JG.
  Title
MAM3 catalyzes the formation of all aliphatic glucosinolate chain lengths in Arabidopsis.
  Journal
Plant Physiol 144:60-71 (2007)
DOI:10.1104/pp.106.091579
  Sequence
[ath:AT5G23020]
Other DBs
ExplorEnz - The Enzyme Database: 2.3.3.17
IUBMB Enzyme Nomenclature: 2.3.3.17
ExPASy - ENZYME nomenclature database: 2.3.3.17
BRENDA, the Enzyme Database: 2.3.3.17

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