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Information on EC 4.2.1.33 - 3-isopropylmalate dehydratase and Organism(s) Pyrococcus horikoshii and UniProt Accession O59393

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.33 3-isopropylmalate dehydratase
IUBMB Comments
Forms part of the leucine biosynthesis pathway. The enzyme brings about the interconversion of the two isomers of isopropylmalate. It contains an iron-sulfur cluster.
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This record set is specific for:
Pyrococcus horikoshii
UNIPROT: O59393
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Word Map
The taxonomic range for the selected organisms is: Pyrococcus horikoshii
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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Synonyms
isopropylmalate isomerase, leucd, alpha-isopropylmalate isomerase, ipmi ssu1, isopropylmalate dehydratase, 3-isopropylmalate dehydratase, ipm isomerase, alpha-ipm isomerase, mj0499, leu1s, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Alpha-IPM isomerase
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alpha-isopropylmalate isomerase
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beta-Isopropylmalate dehydratase
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dehydratase,beta-isopropylmalate
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IPM dehydratase
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IPMI
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isopropylmalate isomerase
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SOI10
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Superoxide-inducible protein 10
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SYSTEMATIC NAME
IUBMB Comments
(2R,3S)-3-isopropylmalate hydro-lyase (2-isopropylmaleate-forming)
Forms part of the leucine biosynthesis pathway. The enzyme brings about the interconversion of the two isomers of isopropylmalate. It contains an iron-sulfur cluster.
CAS REGISTRY NUMBER
COMMENTARY hide
37290-72-5
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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
(2S)-2-isopropylmalate
show the reaction diagram
the isopropylmalate isomerase small subunit of the hyperthermophilic archaea Pyrococcus horikoshii (PhIPMI-s) functions as isopropylmalate isomerase in the leucine biosynthesis pathway, and as homoaconitase (HACN) in the lysine biosynthesis pathway via alpha-aminoadipic acid
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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
(2S)-2-isopropylmalate
show the reaction diagram
the isopropylmalate isomerase small subunit of the hyperthermophilic archaea Pyrococcus horikoshii (PhIPMI-s) functions as isopropylmalate isomerase in the leucine biosynthesis pathway, and as homoaconitase (HACN) in the lysine biosynthesis pathway via alpha-aminoadipic acid
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure isopropylmalate isomerase small subunit. Four molecules create an interlocked assembly with intermolecular disulfide linkages having a skewed 222 point-group symmetry. The structure reveals the formation of intermolecular disulfide linkages, and it provides insight into the dual substrate specificity of the enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yasutake, Y.; Yao, M.; Sakai, N.; Kirita, T.; Tanaka, I.
Crystal structure of the Pyrococcus horikoshii isopropylmalate isomerase small subunit provides insight into the dual substrate specificity of the enzyme
J. Mol. Biol.
344
325-333
2004
Pyrococcus horikoshii (O59393), Pyrococcus horikoshii
Manually annotated by BRENDA team