Reactome: A Curated Pathway Database
THIS SITE IS USED FOR CURATION AND TESTING
IT IS NOT STABLE, IS LINKED TO AN INCOMPLETE DATA SET, AND IS NOT MONITORED FOR PERFORMANCE. WE STRONGLY RECOMMEND THE USE OF OUR PUBLIC SITE

Query author contributions in Reactome

Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.

If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.

Name Email address

Details on Person Cytosolic acetyl-CoA carboxylase 1 (ACACA) catalyzes the rea...

Class:IdSummation:76211
_displayNameCytosolic acetyl-CoA carboxylase 1 (ACACA) catalyzes the rea...
_timestamp2023-02-17 21:17:42
created[InstanceEdit:76206] Gopinathrao, G, 2003-10-03 00:00:00
modified[InstanceEdit:76206] Gopinathrao, G, 2003-10-03 00:00:00
[InstanceEdit:76562] Gopinathrao, G, 2003-10-10 10:53:18
[InstanceEdit:77113] Gopinathrao, G, 2003-10-16 18:43:13
[InstanceEdit:201317] Gopinathrao, G, 2007-08-03 18:51:55
[InstanceEdit:539091] D'Eustachio, P, 2010-03-09
[InstanceEdit:539120] D'Eustachio, P, 2010-03-09
[InstanceEdit:8876895] Jassal, Bijay, 2016-06-17
[InstanceEdit:8878975] Jassal, Bijay, 2016-07-14
[InstanceEdit:9828803] Orlic-Milacic, Marija, 2023-02-17
textCytosolic acetyl-CoA carboxylase 1 (ACACA) catalyzes the reaction of bicarbonate, ATP, and acetyl-CoA to form malonyl-CoA, ADP, and orthophosphate. The reaction is positively regulated by citrate. The human ACACA cDNA has been cloned (Abu-Elheiga et al. 1995) and the biochemical properties of the human enzyme have recently been described (Cheng et al. 2007; Locke et al. 2008). Four ACACA isoforms generated by alternative splicing have been identified as mRNAs - the protein product of the first has been characterized experimentally. ACACA uses biotin (Btn) and two Mn2+ ions per subunit as cofactors and its activity is increased by polymerization (Kim et al. 2010, Ingaramo & Beckett 2012). Cytosolic ACACA is thought to maintain regulation of fatty acid synthesis in all tissues but especially lipogenic tissues such as adipose tissue and lactating mammary glands.

Mid1-interacting protein 1 (MID1IP1, aka MIG12, SPOT14R, S14R) plays a role in the regulation of lipogenesis in the liver. It is rapidly upregulated by processes that induce lipogenesis (enhanced glucose metabolism, thyroid hormone administration) (Tsatsos et al. 2008). MID1IP1 forms a heterodimer with thyroid hormone-inducible hepatic protein (THRSP, aka SPOT14, S14), proposed to play the same role in lipogenesis as MID1IP1 (Aipoalani et al. 2010). This complex can polymerizes in fatty acid (FA) synthesis. Polymerization enhances ACACA and ACACB enzyme activities (Kim et al. 2010).
(summation)[Reaction:75851] Btn-ACACA:2Mn2+ polymer carboxylates Ac-CoA to form Mal-CoA [Homo sapiens]
[Reaction:200555] Formation of Malonyl-CoA from Acetyl-CoA (liver) [Homo sapiens]
[Change default viewing format]
No pathways have been reviewed or authored by Cytosolic acetyl-CoA carboxylase 1 (ACACA) catalyzes the rea... (76211)