Biology:MCAT (gene)

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Malonyl CoA-acyl carrier protein transacylase, mitochondrial is an enzyme that in humans is encoded by the MCAT gene.[1][2]

Function

The protein encoded by this gene is found exclusively in the mitochondrion, where it catalyzes the transfer of a malonyl group from malonyl-CoA to the mitochondrial acyl carrier protein. The encoded protein may be part of a fatty acid synthase complex that is more like the type II prokaryotic and plastid complexes rather than the type I human cytosolic complex. Two transcript variants encoding different isoforms have been found for this gene.[2]

Clinical significance

The enzyme encoded by the MCAT gene, along with other enzymes that regulate Malonyl-CoA concentration, have been shown to regulate levels such that malonyl-CoA concentration decreases in human muscle tissue when under exercise training. This enzyme specifically has increased activity under these conditions, as it is known to catabolize malonyl-CoA. [3]

Interactions

The human Malonyl CoA-acel carrier protein transacylase in human mitochondria associates with respiratory complex one, such that it interacts functionally with a mitochondrial malonyltransferase. Both species are encoded by nuclear genes, and their translocation into mitochondria is dependent on the presence of an N-terminal targeting sequence.[1]

References

  1. 1.0 1.1 "Cloning, expression, characterization, and interaction of two components of a human mitochondrial fatty acid synthase. Malonyltransferase and acyl carrier protein". The Journal of Biological Chemistry 278 (41): 40067–74. Oct 2003. doi:10.1074/jbc.M306121200. PMID 12882974. 
  2. 2.0 2.1 "Entrez Gene: MCAT malonyl CoA:ACP acyltransferase (mitochondrial)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27349. 
  3. "Exercise training decreases the concentration of malonyl-CoA and increases the expression and activity of malonyl-CoA decarboxylase in human muscle". American Journal of Physiology. Endocrinology and Metabolism 290 (6): E1296-303. Jun 2006. doi:10.1152/ajpendo.00341.2005. PMID 16434556. 

Further reading