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EC Tree
IUBMB Comments The product decarboxylates spontaneously to yield 4-methyl-2-oxopentanoate.
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
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NAD-dependent isopropylmalate dehydrogenase
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2-hydroxy-4-methyl-3-carboxyvalerate:NAD+ oxidoreductase
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2R,3S-isopropylmalate:NAD+ oxidoreductase (decaboxylating)
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3-IPM dehydrogenase
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beta-IPM dehydrogenase
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beta-isopropylmalate dehydrogenase
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beta-isopropylmalic enzyme
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dehydrogenase, 3-isopropylmalate
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isopropylmalate dehydrogenase
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threo-Ds-3-isopropylmalate dehydrogenase
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(2R,3S)-3-isopropylmalate:NAD+ oxidoreductase
The product decarboxylates spontaneously to yield 4-methyl-2-oxopentanoate.
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(2R,3S)-3-isopropylmalate + NAD+
(2S)-2-isopropyl-3-oxosuccinate + NADH + H+
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-
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r
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
(S)-malate + NAD+
pyruvate + NADH + CO2
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12% of the activity with 3-isopropylmalate
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-
?
3-ethylmalate + NAD+
3-ethylpyruvate + NADH + CO2
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?
3-isoamylmalate + NAD+
3-isoamylpyruvate + NADH + CO2
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-
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-
?
3-methylmalate + NAD+
3-methylpyruvate + NADH + CO2
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?
3-tert-butylmalate + NAD+
3-tert-butylpyruvate + NADH + CO2
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-
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?
D-malate + NAD+
pyruvate + NADH + CO2
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19% of the activity with 3-isopropylmalate
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?
malate + NAD+
pyruvate + NADH + H+ + CO2
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additional information
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substrate specificity-determining residues, overview
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(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
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?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
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a large movement of domain 1 is induced by substrate binding, which results in the formation of the hydrophobic pocket for the gamma-isopropyl moiety of isopropylmalate
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?
(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
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key enzyme in leucine biosynthesis
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?
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(2R,3S)-3-isopropylmalate + NAD+
2-oxoisocaproate + NADH + H+ + CO2
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key enzyme in leucine biosynthesis
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?
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NAD+
dependent on, cofactor specificity-determining residues, overview
NAD+
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NAD+
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the acidic tip of IPM-Glu88 is likely to interact with the nicotinamide mononucleotide ribose of NAD+ in the ternary complex. This structure clearly explains the substrate specificity of IPMDH
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K+
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monovalent cation required
Mg2+
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1.0 mM, enhances activity 4.7fold
Mn2+
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1.0 mM, enhances activity 4.2fold
NH4+
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monovalent cation required
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iodoacetamide
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5 mM, 50% inhibition
iodoacetate
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5 mM, 50% inhibition
NEM
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5 mM, 50% inhibition
PCMB
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5 mM, 50% inhibition
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0.015 - 0.026
(2R,3S)-3-isopropylmalate
0.074
3-tert-butylmalate
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0.015
(2R,3S)-3-isopropylmalate
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0.026
(2R,3S)-3-isopropylmalate
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pH 9.0
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28
(2R,3S)-3-isopropylmalate
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2.7
3-tert-butylmalate
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gene leuB
SwissProt
brenda
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LEU3_ACIFR
358
0
38462
Swiss-Prot
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38000
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2 * 38000, SDS-PAGE
73000
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equilibrium sedimentation
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dimer
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2 * 38000, SDS-PAGE
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enzyme in complex with 3-isopropylmalate
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70
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10 min, 40% loss of activity
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overexpression in Escherichia coli
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recombinant enzyme expressed in Escherichia coli
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phylogenetic analysis, comparison to isocitrate dehydrogenase, EC 1.1.1.41, overview
expression in Escherichia coli
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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
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brenda
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
brenda
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
brenda
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
brenda
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)
brenda