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Information on EC 1.1.1.85 - 3-isopropylmalate dehydrogenase and Organism(s) Sulfurisphaera tokodaii and UniProt Accession P50455
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1.1.1.85 3-isopropylmalate dehydrogenaseIUBMB Comments
The product decarboxylates spontaneously to yield 4-methyl-2-oxopentanoate.
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Word Map
The taxonomic range for the selected organisms is: Sulfurisphaera tokodaii
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
3-isopropylmalate dehydrogenase, ipmdh, beta-isopropylmalate dehydrogenase, isopropylmalate dehydrogenase, ipmdh2, ipmdh3, beta-ipm dehydrogenase, sbipmdh, ipmdh1, saci_0600, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-hydroxy-4-methyl-3-carboxyvalerate:NAD+ oxidoreductase
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-
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2R,3S-isopropylmalate:NAD+ oxidoreductase (decaboxylating)
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3-IPM dehydrogenase
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3-IPM-DH
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-
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beta-IPM dehydrogenase
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beta-IPMDH
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-
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beta-isopropylmalate dehydrogenase
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-
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beta-isopropylmalic enzyme
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dehydrogenase, 3-isopropylmalate
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IMDH
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IPMDH
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isopropylmalate dehydrogenase
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threo-Ds-3-isopropylmalate dehydrogenase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
(2R,3S)-3-isopropylmalate:NAD+ oxidoreductase
The product decarboxylates spontaneously to yield 4-methyl-2-oxopentanoate.
CAS REGISTRY NUMBER
COMMENTARY
9030-97-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2R,3S)-3-isopropylmalate + NAD+
D-3-isopropyl-2-oxosuccinate + NADH + H+
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-
-
?
D-3-ethylmalate + NAD+
D-3-ethyl-2-oxosuccinate + NADH + H+
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-
-
?
D-3-isobutylmalate + NAD+
D-3-isobutyl-2-oxosuccinate + NADH + H+
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-
-
?
D-3-isopentylmalate + NAD+
D-3-isopentyl-2-oxosuccinate + NADH + H+
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-
-
?
D-3-methylmalate + NAD+
D-3-methyl-2-oxosuccinate + NADH + H+
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-
-
?
D-3-t-butylmalate + NAD+
D-3-t-butyl-2-oxosuccinate + NADH + H+
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-
-
?
(2R,3S)-3-isopropylmalate + NAD+
?
the enzyme is enzyme involved in leucine biosynthesis
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2R,3S)-3-isopropylmalate + NAD+
?
the enzyme is enzyme involved in leucine biosynthesis
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0039
3-isopropylmalate
pH 7.5, 70°C, recombinant mutant F3S/S232G
0.0044
3-isopropylmalate
pH 7.5, 70°C, recombinant mutant L288P
0.0055
3-isopropylmalate
pH 7.5, 70°C, recombinant wild-type enzyme
0.0067
3-isopropylmalate
pH 7.5, 70°C, recombinant mutant F3S/L288P
0.008
3-isopropylmalate
pH 7.5, 70°C, recombinant mutant R284G
0.39
NAD+
pH 7.5, 70°C, recombinant wild-type enzyme and mutant F3S
additional information
additional information
Michaelis-Menten kinetics of recombinant wild-type and mutant enzymes at different temperatures, overview
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additional information
additional information
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Michaelis-Menten kinetics of recombinant wild-type and mutant enzymes at different temperatures, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.8
3-isopropylmalate
pH 7.5, 70°C, recombinant mutant F3S/S232G
6.9
3-isopropylmalate
pH 7.5, 70°C, recombinant wild-type enzyme
7.8
3-isopropylmalate
pH 7.5, 70°C, recombinant mutant F3S/L288P
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
95
96
Tm-value of wild-type enzyme is 96°C. Tm-value of mutant enzyme K152R is 95.6°C. Tm-value of mutant enzyme (M91L/I95L/K152R/G154A/A259S/F261P/Y282L) is 96.4°C
97
99
99
t1/2: 3.67 min (wild-type enzyme), 5.52 min (mutant enzyme M91L/I95L), 6.56 min (K152R/G154A mutant enzyme), 5.72 min (K152R mutant enzyme), 7.13 min (G154A mutant enzyme), 4.79 min (A259S/F261P mutant enzyme), 3.79 min (Y282L mutant enzyme), 6.5 min (M91L/I95L/K152R/G154A/A259S/F261P/Y282L mutant enzyme)
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 95
2% of maximal activity at 25°C, maximal activity at 95°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme is involved in the leucine biosynthetic pathway
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
absence of either intra- or inter-subunit disulfide bonds
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A259S/F261P
Tm-value of mutant enzyme is 1.1°C higher than Tm-value of wild-type enzyme
F145S
random mutagenesis, the mutation alters the Km values for NAD+ and/or the kcat value, the mutant shows reduced thermostability compared to the wild-type enzyme
F3S
random mutagenesis, the mutation alters the Km values for NAD+ and/or the kcat value, the mutant shows reduced thermostability compared to the wild-type enzyme
F3S/L288P
random mutagenesis, the mutation alters the Km values for NAD+ and/or the kcat value, the mutant shows reduced thermostability compared to the wild-type enzyme. The MA153 strain containing a doubly mutated leuB gene grows more rapidly than does Escherichia coli MA153 containing the wild-type leuB gene in leucine-free M9 minimal liquid medium
F3S/S232G
random mutagenesis, the mutation alters the Km values for NAD+ and/or the kcat value, the mutant shows reduced thermostability compared to the wild-type enzyme. The MA153 strain containing a doubly mutated leuB gene grows more rapidly than does Escherichia coli MA153 containing the wild-type leuB gene in leucine-free M9 minimal liquid medium
G154A
Tm-value of mutant enzyme is 1.9°C higher than Tm-value of wild-type enzyme
I68L/I142T/K335E
random mutagenesis, the mutation alters the Km values for NAD+ and/or the kcat value, the mutant shows reduced thermostability compared to the wild-type enzyme
K152R
Tm-value of mutant enzyme is 0.4°C lower than Tm-value of wild-type enzyme
K152R/G154A
Tm-value of mutant enzyme is 1.2°C higher than Tm-value of wild-type enzyme
L288P
random mutagenesis, the mutation alters the Km values for NAD+ and/or the kcat value, the mutant shows reduced thermostability compared to the wild-type enzyme
L328S
random mutagenesis, the mutation alters the Km values for NAD+ and/or the kcat value, the mutant shows reduced thermostability compared to the wild-type enzyme
L336P
random mutagenesis, the mutation alters the Km values for NAD+ and/or the kcat value, the mutant shows reduced thermostability compared to the wild-type enzyme
M91L/I95L
Tm-value of mutant enzyme is 3.2°C higher than Tm-value of wild-type enzyme
M91L/I95L/K152R/G154A/A259S/F261P/Y282L
Tm-value of mutant enzyme is 0.4°C higher than Tm-value of wild-type enzyme
R284G
random mutagenesis, the mutation alters the Km values for NAD+ and/or the kcat value, the mutant shows reduced thermostability compared to the wild-type enzyme
Y282L
Tm-value of mutant enzyme is 0.3°C lower than Tm-value of wild-type enzyme
Y309H
random mutagenesis, the mutation alters the Km values for NAD+ and/or the kcat value, the mutant shows reduced thermostability compared to the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Escherichia coli strain MA153 by anion exchange and hydrophobic interaction chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene leuB, expression of wild-type and mutant enzymes in Escherichia coli strain MA153
wild type and mutant leuB genes are overexpressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Suzuki, T.; Inoki, Y.; Yamagishi, A.; Iwasaki, T.; Wakagi, T.; Oshima, T.
Molecular and phylogenetic characterization of isopropylmalate dehydrogenase of a thermoacidophilic archaeon, Sulfolobus sp. strain 7
J. Bacteriol.
179
1174-1179
1997
Sulfurisphaera tokodaii (P50455), Sulfurisphaera tokodaii 7 (P50455)
Sasaki, M.; Uno, M.; Akanuma, S.; Yamagishi, A.
Random mutagenesis improves the low-temperature activity of the tetrameric 3-isopropylmalate dehydrogenase from the hyperthermophile Sulfolobus tokodaii
Protein Eng. Des. Sel.
21
721-727
2008
Sulfurisphaera tokodaii (P50455), Sulfurisphaera tokodaii
Miyazaki, J.; Nakaya, S.; Suzuki, T.; Tamakoshi, M.; Oshima, T.; Yamagishi, A.
Ancestral residues stabilizing 3-isopropylmalate dehydrogenase of an extreme thermophile: experimental evidence supporting the thermophilic common ancestor hypothesis
J. Biochem.
129
777-782
2001
Sulfurisphaera tokodaii (P50455), Sulfurisphaera tokodaii 7 (P50455)
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