3-hydroxyisobutyrate dehydrogenase
(Redirected from HIBADH)
| 3-hydroxyisobutyrate dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.31 | ||||||||
| CAS no. | 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 / QuickGO | ||||||||
| |||||||||
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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:
[[File:No image file is associated with 3-Hydroxyisobutyric acid via Wikidata. Try a qualifier ID or use chemrxn/subunit.|frameless|class=skin-invert-image|alt=2D representation of the chemical structure of 3-Hydroxyisobutyric acid .]]
+ NAD+
H+
H+
[[File:No image file is associated with Methylmalonic acid semialdehyde via Wikidata. Try a qualifier ID or use chemrxn/subunit.|frameless|class=skin-invert-image|alt=2D representation of the chemical structure of Methylmalonic acid semialdehyde .]]
+ NADPH
The two substrates of this enzyme are 3-hydroxyisobutyric acid and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are methylmalonic acid semialdehyde, reduced NADH, and a proton.[3]
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 | edit source]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 | edit source]As of late 2007, five structures have been solved for this class of enzymes, with PDB accession codes 1WP4, 2CVZ, 2GF2, 2H78, and 2I9P.
References
[edit | edit source]Further reading
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External links
[edit | edit source]- Human HIBADH genome location and HIBADH gene details page in the UCSC Genome Browser.
- PDBe-KB provides an overview of all the structure information available in the PDB for Human 3-hydroxyisobutyrate dehydrogenase, mitochondrial
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