KEGG ENZYME: 2.3.3.17

ENZYME: 2.3.3.17

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

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)

(other) R08619 R08623 R08627 R08631 R08640 R08644

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:	9308098 9308099 9308100

CRB:	17881318 17883723 17883860

CSAT:

104706601 104706602 104706603 104736315 104736316 104736317 104770650 104770651 104770652

EUS:	EUTSA_v10003976mg EUTSA_v10004072mg EUTSA_v10005522mg

BRP:	103853322 103854915 103860537(MAM3-1) 103860538(MAM1-1) 103861112

BNA:	106377268 106377269 106382716 106434595 106434598 106434605 106444270

BOE:	106301761 106324531 106324637 106325524

RSZ:	108813467 108835158 108848454 130497108 130507828

QSA:	O6P43_017013 O6P43_017014

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