3-hydroxyisobutyrate dehydrogenase

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3-hydroxyisobutyrate dehydrogenase
Identifiers
EC number 1.1.1.31
CAS number 9028-39-1
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
HIBADH
Protein HIBADH PDB 2gf2.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases HIBADH, Hibadh, 6430402H10Rik, AI265272, NS5ATP1, 3-hydroxyisobutyrate dehydrogenase
External IDs MGI: 1889802 HomoloGene: 15088 GeneCards: 11112
EC number 1.1.1.31
RNA expression pattern
PBB GE HIBADH gnf1h05976 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_152740

NM_145567

RefSeq (protein)

NP_689953.1

NP_663542.1

Location (UCSC) Chr 7: 27.53 – 27.66 Mb Chr 6: 52.55 – 52.64 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

In enzymology, a 3-hydroxyisobutyrate dehydrogenase (EC 1.1.1.31) also known as β-hydroxyisobutyrate dehydrogenase or 3-hydroxyisobutyrate dehydrogenase, mitochondrial (HIBADH) is an enzyme[1] that in humans is encoded by the HIBADH gene.[2]

3-Hydroxyisobutyrate dehydrogenase catalyzes the chemical reaction:

3-hydroxy-2-methylpropanoate + NAD+ 2-methyl-3-oxopropanoate + NADH + H+

Thus, the two substrates of this enzyme are 3-hydroxy-2-methylpropanoate and NAD+, whereas its 3 products are 2-methyl-3-oxopropanoate, NADH, and H+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-hydroxy-2-methylpropanoate:NAD+ oxidoreductase. This enzyme participates in valine, leucine and isoleucine degradation.

Function[edit]

3-hydroxyisobutyrate dehydrogenase is a tetrameric mitochondrial enzyme that catalyzes the NAD+-dependent, reversible oxidation of 3-hydroxyisobutyrate, an intermediate of valine catabolism, to methylmalonate semialdehyde.[2]

Structural studies[edit]

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1WP4, 2CVZ, 2GF2, 2H78, and 2I9P.

References[edit]

  1. ^ Robinson WG, Coon MJ (March 1957). "The purification and properties of beta-hydroxyisobutyric dehydrogenase". J. Biol. Chem. 225 (1): 511–21. PMID 13416257. 
  2. ^ a b "Entrez Gene: HIBADH 3-hydroxyisobutyrate dehydrogenase". 

Further reading[edit]