Acetyl-CoA carboxylase

acetyl-CoA carboxylase
Human ACC1 homodimer with catalytic domains highlighted; biotin carboxylase (red), biotinyl-binding (blue) and carboxyltransferase (green). PDB: 6G2D
Identifiers
EC no.6.4.1.2
CAS no.9023-93-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Acetyl-CoA carboxylase alpha
Identifiers
SymbolACACA
Alt. symbolsACAC, ACC1, ACCA
NCBI gene31
HGNC84
OMIM601557
RefSeqNM_198839
UniProtQ13085
Other data
EC number6.4.1.2
LocusChr. 17 q21
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StructuresSwiss-model
DomainsInterPro
Acetyl-CoA carboxylase beta
Identifiers
SymbolACACB
Alt. symbolsACC2, ACCB
NCBI gene32
HGNC85
OMIM200350
RefSeqNM_001093
UniProtO00763
Other data
EC number6.4.1.2
LocusChr. 12 q24.1
Search for
StructuresSwiss-model
DomainsInterPro

Acetyl-CoA carboxylase (ACC) is a biotin-dependent enzyme (EC 6.4.1.2) that catalyzes the irreversible carboxylation of acetyl-CoA to produce malonyl-CoA through its two catalytic activities, biotin carboxylase (BC) and carboxyltransferase (CT). ACC is a multi-subunit enzyme in most prokaryotes and in the chloroplasts of most plants and algae, whereas it is a large, multi-domain enzyme in the cytoplasm of most eukaryotes. The most important function of ACC is to provide the malonyl-CoA substrate for the biosynthesis of fatty acids.[1] The activity of ACC can be controlled at the transcriptional level as well as by small molecule modulators and covalent modification. The human genome contains the genes for two different ACCs[2]ACACA[3] and ACACB.[4]

  1. ^ Tong L (August 2005). "Acetyl-coenzyme A carboxylase: crucial metabolic enzyme and attractive target for drug discovery". Cellular and Molecular Life Sciences. 62 (16): 1784–1803. doi:10.1007/s00018-005-5121-4. PMC 11139103. PMID 15968460. S2CID 1131957.
  2. ^ Brownsey RW, Zhande R, Boone AN (November 1997). "Isoforms of acetyl-CoA carboxylase: structures, regulatory properties and metabolic functions". Biochemical Society Transactions. 25 (4): 1232–1238. doi:10.1042/bst0251232. PMID 9449982.
  3. ^ Abu-Elheiga L, Jayakumar A, Baldini A, Chirala SS, Wakil SJ (April 1995). "Human acetyl-CoA carboxylase: characterization, molecular cloning, and evidence for two isoforms". Proceedings of the National Academy of Sciences of the United States of America. 92 (9): 4011–4015. Bibcode:1995PNAS...92.4011A. doi:10.1073/pnas.92.9.4011. PMC 42092. PMID 7732023.
  4. ^ Widmer J, Fassihi KS, Schlichter SC, Wheeler KS, Crute BE, King N, et al. (June 1996). "Identification of a second human acetyl-CoA carboxylase gene". The Biochemical Journal. 316 (Pt 3): 915–922. doi:10.1042/bj3160915. PMC 1217437. PMID 8670171.