Gamma-butyrobetaine dioxygenase

gamma-butyrobetaine dioxygenase
Identifiers
EC number	1.14.11.1
CAS number	9045-31-2
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
Search PMC articles PubMed articles

Butyrobetaine (gamma), 2-oxoglutarate dioxygenase (gamma-butyrobetaine hydroxylase) 1
Rendering based on PDB 3MS5.
Available structures PDB 3MS5, 3N6W, 3O2G
Identifiers
Symbols	BBOX1; BBH; BBOX; G-BBH; gamma-BBH
External IDs	OMIM: 603312 MGI: 1891372 HomoloGene: 2967 GeneCards: BBOX1 Gene
EC number	1.14.11.1
Gene Ontology Molecular function • iron ion binding • zinc ion binding • gamma-butyrobetaine dioxygenase activity • gamma-butyrobetaine dioxygenase activity • gamma-butyrobetaine dioxygenase activity • oxidoreductase activity • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen • metal ion binding Cellular component • cytoplasm • cytosol • actin cytoskeleton • intracellular membrane-bounded organelle Biological process • cellular nitrogen compound metabolic process • carnitine biosynthetic process • carnitine biosynthetic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8424	170442
Ensembl	ENSG00000129151	ENSMUSG00000041660
UniProt	O75936	Q924Y0
RefSeq (mRNA)	NM_003986	NM_130452.1
RefSeq (protein)	NP_003977	NP_569719.1
Location (UCSC)	Chr 11: 27.06 – 27.15 Mb	Chr 2: 110.1 – 110.15 Mb
PubMed search	[1]	[2]

Gamma-butyrobetaine dioxygenase is an enzyme that in humans is encoded by the BBOX1 gene. Gamma-butyrobetaine dioxygenase catalyzes the formation of L-carnitine from gamma-butyrobetaine, the last step in the L-carnitine biosynthetic pathway. Carnitine is essential for the transport of activated fatty acids across the mitochondrial membrane during mitochondrial beta-oxidation.

Reaction

The following reaction is catalyzed by gamma-butyrobetaine dioxygenase:

4-trimethylammoniobutanoate + 2-oxoglutarate + O₂ $\rightleftharpoons$ 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO₂

The 3 substrates of this enzyme are 4-trimethylammoniobutanoate, 2-oxoglutarate, and O₂, whereas its 3 products are 3-hydroxy-4-trimethylammoniobutanoate, succinate, and CO₂.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O₂ as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O₂ with 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor. This enzyme participates in lysine degradation. It has 2 cofactors: iron, and Ascorbate.

See Also

• L-Carnitine
• Beta Oxidation
• Fatty acid metabolism

Further reading

• Rebouche CJ (1992). "Ascorbic acid and carnitine biosynthesis.". Am. J. Clin. Nutr. 54 (6 Suppl): 1147S–1152S. PMID 1962562. 
• Paul HS, Sekas G, Adibi SA (1992). "Carnitine biosynthesis in hepatic peroxisomes. Demonstration of gamma-butyrobetaine hydroxylase activity.". Eur. J. Biochem. 203 (3): 599–605. doi:10.1111/j.1432-1033.1992.tb16589.x. PMID 1735445. 
• Olson AL, Rebouche CJ (1987). "gamma-Butyrobetaine hydroxylase activity is not rate limiting for carnitine biosynthesis in the human infant.". J. Nutr. 117 (6): 1024–31. PMID 3110383. 
• Wehbie RS, Punekar NS, Lardy HA (1988). "Rat liver gamma-butyrobetaine hydroxylase catalyzed reaction: influence of potassium, substrates, and substrate analogues on hydroxylation and decarboxylation.". Biochemistry 27 (6): 2222–8. doi:10.1021/bi00406a062. PMID 3378057. 
• Lindstedt S, Nordin I (1984). "Multiple forms of gamma-butyrobetaine hydroxylase (EC 1.14.11.1).". Biochem. J. 223 (1): 119–27. PMC 1144272. PMID 6497835. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1144272. 
• Lindstedt G, Lindstedt S, Nordin I (1983). "Gamma-butyrobetaine hydroxylase in human kidney.". Scand. J. Clin. Lab. Invest. 42 (6): 477–85. PMID 7156861. 
• Galland S, Le Borgne F, Bouchard F, et al. (1999). "Molecular cloning and characterization of the cDNA encoding the rat liver gamma-butyrobetaine hydroxylase.". Biochim. Biophys. Acta 1441 (1): 85–92. PMID 10526231. 
• 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. 
• 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. 
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356129. 
• Rigault C, Le Borgne F, Demarquoy J (2007). "Genomic structure, alternative maturation and tissue expression of the human BBOX1 gene.". Biochim. Biophys. Acta 1761 (12): 1469–81. doi:10.1016/j.bbalip.2006.09.014. PMID 17110165. 
• Lindstedt G, Lindstedt S (1970). "Cofactor requirements of gamma-butyrobetaine hydroxylase from rat liver". J. Biol. Chem. 245 (16): 4178–86. PMID 4396068.