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Information on EC 1.1.1.85 - 3-isopropylmalate dehydrogenase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WKK9

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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:
Mycobacterium tuberculosis
UNIPROT: P9WKK9
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Word Map
The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The enzyme appears in selected viruses and cellular organisms
Synonyms
3-isopropylmalate dehydrogenase, ipmdh, beta-isopropylmalate dehydrogenase, isopropylmalate dehydrogenase, ipmdh2, ipmdh3, ipmdh1, beta-ipm dehydrogenase, sbipmdh, soipmdh, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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3-IPM-DH
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beta-IPM dehydrogenase
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beta-IPMDH
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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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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 hide
LITERATURE
redox reaction
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oxidation
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reduction
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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 hide
9030-97-1
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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+
2-isopropyl-3-oxosuccinate + NADH + H+
show the reaction diagram
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
O-isobutenyloxalylhydroxamate
O-isobutenyloxalylhydroxamate binds to the active site of enzyme in a mode similar to the substrate isopropylmalate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
The crystal structure is determined at 1.65 A resolution. The crystals contain two functional dimers in the asymmetric unit in an arrangement close to a tetramer of D2 symmetry.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Singh, R.K.; Kefala, G.; Janowski, R.; Mueller-Dieckmann, C.; von Kries, J.P.; Weiss, M.S.
The High-resolution Structure of LeuB (Rv2995c) from Mycobacterium tuberculosis
J. Mol. Biol.
346
1-11
2005
Mycobacterium tuberculosis (P9WKK9), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WKK9)
Manually annotated by BRENDA team