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Information on EC 1.1.1.85 - 3-isopropylmalate dehydrogenase and Organism(s) Acidithiobacillus ferrooxidans and UniProt Accession Q56268

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IUBMB Comments
The product decarboxylates spontaneously to yield 4-methyl-2-oxopentanoate.
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This record set is specific for:
Acidithiobacillus ferrooxidans
UNIPROT: Q56268
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Word Map
The taxonomic range for the selected organisms is: Acidithiobacillus ferrooxidans
The enzyme appears in selected viruses and cellular organisms
Synonyms
3-isopropylmalate dehydrogenase, ipmdh, beta-isopropylmalate dehydrogenase, isopropylmalate dehydrogenase, ipmdh2, ipmdh3, sbipmdh, ipmdh1, beta-ipm dehydrogenase, soipmdh, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NAD-dependent isopropylmalate dehydrogenase
-
2-hydroxy-4-methyl-3-carboxyvalerate:NAD+ oxidoreductase
-
-
-
-
2R,3S-isopropylmalate:NAD+ oxidoreductase (decaboxylating)
-
-
-
-
3-IPM dehydrogenase
-
-
-
-
3-IPM-DH
-
-
-
-
beta-IPM dehydrogenase
-
-
-
-
beta-IPMDH
-
-
-
-
beta-isopropylmalate dehydrogenase
-
-
-
-
beta-isopropylmalic enzyme
-
-
-
-
dehydrogenase, 3-isopropylmalate
-
-
-
-
IMDH
-
-
-
-
IPMDH
-
-
-
-
isopropylmalate dehydrogenase
-
-
-
-
threo-Ds-3-isopropylmalate dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(2R,3S)-3-isopropylmalate:NAD+ oxidoreductase
The product decarboxylates spontaneously to yield 4-methyl-2-oxopentanoate.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-97-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R,3S)-3-isopropylmalate + NAD+
(2S)-2-isopropyl-3-oxosuccinate + NADH + H+
show the reaction diagram
-
-
-
-
r
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
show the reaction diagram
(S)-malate + NAD+
pyruvate + NADH + CO2
show the reaction diagram
-
12% of the activity with 3-isopropylmalate
-
-
?
3-ethylmalate + NAD+
3-ethylpyruvate + NADH + CO2
show the reaction diagram
-
-
-
-
?
3-isoamylmalate + NAD+
3-isoamylpyruvate + NADH + CO2
show the reaction diagram
-
-
-
-
?
3-methylmalate + NAD+
3-methylpyruvate + NADH + CO2
show the reaction diagram
-
-
-
-
?
3-tert-butylmalate + NAD+
3-tert-butylpyruvate + NADH + CO2
show the reaction diagram
-
-
-
-
?
D-malate + NAD+
pyruvate + NADH + CO2
show the reaction diagram
-
19% of the activity with 3-isopropylmalate
-
-
?
malate + NAD+
pyruvate + NADH + H+ + CO2
show the reaction diagram
-
-
-
-
?
additional information
?
-
substrate specificity-determining residues, overview
-
-
?
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
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
show the reaction diagram
-
key enzyme in leucine biosynthesis
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
dependent on, cofactor specificity-determining residues, overview
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
-
monovalent cation required
Mg2+
-
1.0 mM, enhances activity 4.7fold
Mn2+
-
1.0 mM, enhances activity 4.2fold
NH4+
-
monovalent cation required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iodoacetamide
-
5 mM, 50% inhibition
iodoacetate
-
5 mM, 50% inhibition
NEM
-
5 mM, 50% inhibition
PCMB
-
5 mM, 50% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015 - 0.026
(2R,3S)-3-isopropylmalate
0.013
3-ethylmalate
-
-
0.11
3-isoamylmalate
-
-
0.05
3-methylmalate
-
-
0.074
3-tert-butylmalate
-
-
12
L-malate
-
pH 9.0
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
28
(2R,3S)-3-isopropylmalate
-
-
38
3-ethylmalate
-
-
20
3-isoamylmalate
-
-
28
3-methylmalate
-
-
2.7
3-tert-butylmalate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene leuB
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LEU3_ACIFR
358
0
38462
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38000
-
2 * 38000, SDS-PAGE
58000
-
gel filtration
73000
-
equilibrium sedimentation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 38000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in complex with 3-isopropylmalate
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
-
10 min, 40% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
-
recombinant enzyme expressed in Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
phylogenetic analysis, comparison to isocitrate dehydrogenase, EC 1.1.1.41, overview
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Inagaki, K.; Kawaguchi, H.; Kuwata, Y.; Sugio, T.; Tanaka, H.; Tano, T.
Cloning and expression of the Thiobacillus ferrooxidans 3-isopropylmalate dehydrogenase gene in Escherichia coli
J. Ferment. Bioeng.
70
71-74
1990
Acidithiobacillus ferrooxidans
-
Manually annotated by BRENDA team
Matsunami, H.; Kawaguchi, H.; Inagaki, K.; Eguchi, T.; Kakinuma, K.; Tanaka, H.
Overproduction and substrate specificity of 3-isopropylmalate dehydrogenase from Thiobacillus ferrooxidans
Biosci. Biotechnol. Biochem.
62
372-373
1998
Acidithiobacillus ferrooxidans
Manually annotated by BRENDA team
Kawaguchi, H.; Inagaki, K.; Kuwata, Y.; Tanaka, H.; Tano, T.
3-Isopropylmalate dehydrogenase from chemolithoautotroph Thiobacillus ferrooxidans: DNA sequence, enzyme purification, and characterization
J. Biochem.
114
370-377
1993
Acidithiobacillus ferrooxidans
Manually annotated by BRENDA team
Imada, K.; Inagaki, K.; Matsunami, H.; Kawaguchi, H.; Tanaka, H.; Tanaka, N.; Namba, K.
Structure of 3-isopropylmalate dehydrogenase in complex with 3-isopropylmalate at 2.0 A resolution: the role of Glu88 in the unique substrate-recognition mechanism
Structure
6
971-982
1998
Acidithiobacillus ferrooxidans
Manually annotated by BRENDA team
Kalinina, O.V.; Gelfand, M.S.
Amino acid residues that determine functional specificity of NADP- and NAD-dependent isocitrate and isopropylmalate dehydrogenases
Proteins
64
1001-1009
2006
Acidithiobacillus ferrooxidans (Q56268), Agrobacterium tumefaciens (P24404), Arthrospira platensis (Q00412), Aspergillus niger (P87256), Azotobacter vinelandii (P96197), Bacteroides fragilis (P54354), Brassica napus (P29102), Candida maltosa (P07139), Clostridium pasteurianum (P31958), Cyberlindnera jadinii (P08791), Eremothecium gossypii (O60027), Escherichia coli (P30125), Leptospira interrogans (P24015), Mycobacterium tuberculosis variant bovis (P94929), Ogataea angusta (P34733), Saccharomyces cerevisiae (P87267), Salmonella enterica subsp. enterica serovar Typhimurium (P37412), Scheffersomyces stipitis (O94114), Thermus aquaticus (P24098), Thermus thermophilus (P61494), Thermus thermophilus (P61495), Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 (P61494), Zymoseptoria tritici (Q9Y897), [Candida] boidinii (Q01987)
Manually annotated by BRENDA team