3-hydroxyisobutyrate dehydrogenase

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3-hydroxyisobutyrate dehydrogenase

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3-hydroxyisobutyrate dehydrogenase

Identifiers

Databases

PDB structures

AmiGO / EGO

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PubMed	articles

3-hydroxyisobutyrate dehydrogenase

PDB rendering based on 2gf2.

Available structures
PDB	2GF2, 2I9P

Identifiers

Symbols

HIBADH; MGC40361; NS5ATP1

External IDs

OMIM: 608475 MGI: 1889802 HomoloGene: 15088 GeneCards: HIBADH Gene

EC number

1.1.1.31

Gene Ontology
Molecular function	• phosphogluconate dehydrogenase (decarboxylating) activity • binding • 3-hydroxyisobutyrate dehydrogenase activity • 3-hydroxyisobutyrate dehydrogenase activity • oxidoreductase activity • NAD binding
Cellular component	• mitochondrion • mitochondrial matrix
Biological process	• pentose-phosphate shunt • valine metabolic process • branched chain family amino acid catabolic process • cellular nitrogen compound metabolic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 7:
27.57 – 27.7 Mb

Chr 6:
52.5 – 52.59 Mb

PubMed search

[1]

[2]

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⁺ $\rightleftharpoons$ 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.

Contents

1 Function
2 Structural studies
3 References
4 Further reading

Function

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

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

^ Robinson WG, Coon MJ (March 1957). "The purification and properties of beta-hydroxyisobutyric dehydrogenase". J. Biol. Chem. 225 (1): 511–21. PMID 13416257.
^ ^a ^b "Entrez Gene: HIBADH 3-hydroxyisobutyrate dehydrogenase". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11112.

Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
Hillier LW, Fulton RS, Fulton LA, et al. (2003). "The DNA sequence of human chromosome 7.". Nature 424 (6945): 157–64. doi:10.1038/nature01782. PMID 12853948.
Scherer SW, Cheung J, MacDonald JR, et al. (2003). "Human chromosome 7: DNA sequence and biology.". Science 300 (5620): 767–72. doi:10.1126/science.1083423. PMC 2882961. PMID 12690205. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2882961.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
"Toward a complete human genome sequence.". Genome Res. 8 (11): 1097–108. 1999. doi:10.1101/gr.8.11.1097. PMID 9847074.
Hughes GJ, Frutiger S, Paquet N, et al. (1994). "Human liver protein map: update 1993.". Electrophoresis 14 (11): 1216–22. doi:10.1002/elps.11501401181. PMID 8313870.
Rougraff PM, Paxton R, Kuntz MJ, et al. (1988). "Purification and characterization of 3-hydroxyisobutyrate dehydrogenase from rabbit liver.". J. Biol. Chem. 263 (1): 327–31. PMID 3335502.
Rougraff PM, Zhang B, Kuntz MJ, et al. (1989). "Cloning and sequence analysis of a cDNA for 3-hydroxyisobutyrate dehydrogenase. Evidence for its evolutionary relationship to other pyridine nucleotide-dependent dehydrogenases.". J. Biol. Chem. 264 (10): 5899–903. PMID 2647728.

PDB gallery

2gf2: Crystal structure of human hydroxyisobutyrate dehydrogenase

2i9p: Crystal structure of human hydroxyisobutyrate dehydrogenase complexed with NAD+

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