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Information on EC 2.3.3.13 - 2-isopropylmalate synthase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9FG67

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EC Tree
IUBMB Comments
Requires K+.
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q9FG67
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Synonyms
alpha-isopropylmalate synthase, isopropylmalate synthase, 2-isopropylmalate synthase, mtipms, alpha-ipms, osipms1, rol17, alpha-isopropylmalate synthetase, alpha-ipm synthase, alpha-ipms-14cr, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-isopropylmalate synthase 1, chloroplastic
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2-isopropylmalate synthase 2, chloroplastic
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3-hydroxy-4-methyl-3-carboxy-pentanoate 2-oxo-3-methyl-butanoate lyase (CoA-acetylating)
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-
-
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3-hydroxy-4-methyl-3-carboxyvalerate 2-oxo-3-methyl-butyrate lyase (CoA-acetylating)
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-
-
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alpha-IPM synthase
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-
-
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Alpha-IPM synthetase
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-
-
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Alpha-isopropylmalate synthase
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-
-
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alpha-isopropylmalate synthase I
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-
-
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alpha-isopropylmalate synthase II
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-
-
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alpha-isopropylmalate synthetase
-
-
-
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alpha-isopropylmalic synthetase
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-
-
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IPM synthase
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-
-
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IPM-synthase
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-
-
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IPMS
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-
-
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isopropylmalate synthase
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-
-
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isopropylmalate synthase 1
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isopropylmalate synthetase
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-
-
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synthase, 2-isopropylmalate
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-
-
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synthase, alpha-isopropylmalate
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldol condensation
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:3-methyl-2-oxobutanoate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming)
Requires K+.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-98-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxo-3-methylbutanoate + acetyl-CoA + H2O
3-hydroxy-4-methyl-3-carboxypentanoate + CoA
show the reaction diagram
-
-
?
2-oxo-3-methylbutanoate + acetyl-CoA + H2O
?
show the reaction diagram
first enzyme in biosynthesis of L-Leu
-
-
?
2-oxo-3-methylbutanoate + acetyl-CoA + H2O
3-hydroxy-4-methyl-3-carboxypentanoate + CoA
show the reaction diagram
2-oxo-3-methylbutanoate + acetyl-CoA + H2O
?
show the reaction diagram
first enzyme in biosynthesis of L-Leu
-
-
?
2-oxo-butanoate + acetyl-CoA + H2O
2-ethyl-2-hydroxysuccinic acid + CoA
show the reaction diagram
2-oxo-n-pentanoate + acetyl-CoA + H2O
2-hydroxy-2-propylsuccinic acid + CoA
show the reaction diagram
isoform IPMS1, 27.2% of the rate with 2-oxo-3-methylbutanoate, isoform IPMS2, 33.8% of the rate with 2-oxo-3-methylbutanoate
-
-
?
2-oxovalerate + acetyl-CoA + H2O
?
show the reaction diagram
4-methylthio-2-oxopentanoate + acetyl-CoA + H2O
? + CoA
show the reaction diagram
-
at very low rate, reaction is involved in glucosinolate chain elongation
-
?
pyruvate + acetyl-CoA + H2O
2-hydroxy-2-methylsuccinic acid + CoA
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-oxo-3-methylbutanoate + acetyl-CoA + H2O
?
show the reaction diagram
first enzyme in biosynthesis of L-Leu
-
-
?
2-oxo-3-methylbutanoate + acetyl-CoA + H2O
?
show the reaction diagram
first enzyme in biosynthesis of L-Leu
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
4 mM, slight stimulation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
10 mM, complete loss of activity
Leu
inhibition of both enzymes reaches a maximum of 30% to 35% around 1 mM Leu
leucine
1 mM, 30-35% inhibition, both isoforms IPMS1 and IPMS2
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.279 - 0.304
2-oxo-3-methylbutanoate
0.016 - 0.045
acetyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.3 - 2.4
2-oxo-3-methylbutanoate
1.9 - 2.2
acetyl-CoA
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
IMS 3
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
mutations in the Arabidopsis ROL17/isopropylmalate synthase 1 locus alter amino acid content, modify the TOR network, and suppress the root hair cell development mutant lrx1
metabolism
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MAM1_ARATH
506
0
55125
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
124000
280000
62300
2 * 62300, calculated from nucleotide sequence
63100
2 * 63100, calculated, isoform IPMS1 with His-tag
64100
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
tetramer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Junk, D.J.; Mourad, G.S.
Isolation and expression analysis of the isopropylmalate synthase gene family of Arabidopsis thaliana
J. Exp. Bot.
53
2453-2454
2002
Arabidopsis thaliana (Q9C550), Arabidopsis thaliana (Q9FG67), Arabidopsis thaliana (Q9FN52), Arabidopsis thaliana, Arabidopsis thaliana IMS 2 (Q9FN52), Arabidopsis thaliana IMS 3 (Q9FG67), Arabidopsis thaliana IMS 1 (Q9C550)
Manually annotated by BRENDA team
de Kraker, J.W.; Luck, K.; Textor, S.; Tokuhisa, J.G.; Gershenzon, J.
Two Arabidopsis genes (IPMS1 and IPMS2) encode isopropylmalate synthase, the branchpoint step in the biosynthesis of leucine
Plant Physiol.
143
970-986
2007
Arabidopsis thaliana, Arabidopsis thaliana (Q9C550), Arabidopsis thaliana (Q9LPR4)
Manually annotated by BRENDA team
Schaufelberger, M.; Galbier, F.; Herger, A.; de Brito Francisco, R.; Roffler, S.; Clement, G.; Diet, A.; Hoertensteiner, S.; Wicker, T.; Ringli, C.
Mutations in the Arabidopsis ROL17/isopropylmalate synthase 1 locus alter amino acid content, modify the TOR network, and suppress the root hair cell development mutant lrx1
J. Exp. Bot.
70
2313-2323
2019
Arabidopsis thaliana (Q9LPR4), Arabidopsis thaliana
Manually annotated by BRENDA team
Xing, A.; Last, R.L.
A regulatory hierarchy of the Arabidopsis branched-chain amino acid metabolic network
Plant Cell
29
1480-1499
2017
Arabidopsis thaliana (Q9LPR4), Arabidopsis thaliana
Manually annotated by BRENDA team