ACSM2B

Acyl-coenzyme A synthetase ACSM2B, mitochondrial is an enzyme that in humans is encoded by the ACSM2B gene.[3][4]

ACSM2B
Identifiers
Aliases	ACSM2B, ACSM2, HXMA, HYST1046, acyl-CoA synthetase medium-chain family member 2B, acyl-CoA synthetase medium chain family member 2B
External IDs	OMIM: 614359 HomoloGene: 89289 GeneCards: ACSM2B
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16p12.3 Start 20,536,226 bp[1] End 20,576,427 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • nucleotide binding • ligase activity • catalytic activity • ATP binding • metal ion binding • butyrate-CoA ligase activity • CoA-ligase activity • acyl-CoA ligase activity • fatty-acyl-CoA synthase activity • fatty acid ligase activity • molecular function Cellular component • mitochondrion • mitochondrial matrix Biological process • xenobiotic metabolic process • metabolism • fatty acid metabolic process • lipid metabolism • fatty acid biosynthetic process • acyl-CoA metabolic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	348158	n/a
Ensembl	ENSG00000066813	n/a
UniProt	Q68CK6	n/a
RefSeq (mRNA)	NM_001105069 NM_182617	n/a
RefSeq (protein)	NP_001098539 NP_872423	n/a
Location (UCSC)	Chr 16: 20.54 – 20.58 Mb	n/a
PubMed search	[2]	n/a
Wikidata
View/Edit Human

References

1. GRCh38: Ensembl release 89: ENSG00000066813 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. Vessey DA, Lau E, Kelley M, Warren RS (Mar 2003). "Isolation, sequencing, and expression of a cDNA for the HXM-A form of xenobiotic/medium-chain fatty acid:CoA ligase from human liver mitochondria". J Biochem Mol Toxicol. 17 (1): 1–6. doi:10.1002/jbt.10056. PMID 12616642.
4. "Entrez Gene: ACSM2 acyl-CoA synthetase medium-chain family member 2".

External links

• Human ACSM2B genome location and ACSM2B gene details page in the UCSC Genome Browser.

Further reading

• Lindner I, Rubin D, Helwig U, et al. (2006). "The L513S polymorphism in medium-chain acyl-CoA synthetase 2 (MACS2) is associated with risk factors of the metabolic syndrome in a Caucasian study population". Mol Nutr Food Res. 50 (3): 270–4. doi:10.1002/mnfr.200500241. PMID 16521160.
• Yamada S, Ohira M, Horie H, et al. (2004). "Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas". Oncogene. 23 (35): 5901–11. doi:10.1038/sj.onc.1207782. PMID 15221005.
• Vessey DA, Kelley M, Warren RS (2004). "Characterization of triacsin C inhibition of short-, medium-, and long-chain fatty acid: CoA ligases of human liver". J. Biochem. Mol. Toxicol. 18 (2): 100–6. doi:10.1002/jbt.20009. PMID 15122652.
• Vessey DA, Kelley M (2001). "Characterization of the reaction mechanism for the XL-I form of bovine liver xenobiotic/medium-chain fatty acid:CoA ligase". Biochem. J. 357 (Pt 1): 283–8. doi:10.1042/0264-6021:3570283. PMC 1221953. PMID 11415461.
• Vessey DA, Kelley M, Warren RS (1999). "Characterization of the CoA ligases of human liver mitochondria catalyzing the activation of short- and medium-chain fatty acids and xenobiotic carboxylic acids". Biochim. Biophys. Acta. 1428 (2–3): 455–62. doi:10.1016/s0304-4165(99)00088-4. PMID 10434065.
• Vessey DA, Hu J (1997). "Isolation from bovine liver mitochondria and characterization of three distinct carboxylic acid: CoA ligases with activity toward xenobiotics". J. Biochem. Toxicol. 10 (6): 329–37. doi:10.1002/jbt.2570100608. PMID 8934636.
• Vessey DA, Hu J, Kelley M (1997). "Interaction of salicylate and ibuprofen with the carboxylic acid: CoA ligases from bovine liver mitochondria". J. Biochem. Toxicol. 11 (2): 73–8. doi:10.1002/(SICI)1522-7146(1996)11:2<73::AID-JBT4>3.0.CO;2-R. PMID 8884467.