Fatty-acyl-CoA synthase

In enzymology, a fatty-acyl-CoA synthase (EC 2.3.1.86) is an enzyme that catalyzes the chemical reaction

acetyl-CoA + n malonyl-CoA + 2n NADH + 2n NADPH + 4n H⁺ long-chain-acyl-CoA + n CoA + n CO₂ + 2n NAD⁺ + 2n NADP⁺

The 5 substrates of this enzyme are acetyl-CoA, malonyl-CoA, NADH, NADPH, and H⁺, whereas its 5 products are long-chain-acyl-CoA, CoA, CO₂, NAD⁺, and NADP⁺.

This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl- reducing). This enzyme is also called yeast fatty acid synthase. This enzyme participates in fatty acid biosynthesis.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2PFF and 2UV8.

References

• Schweizer E, Kniep B, Castorph H, Holzner U (1973). "Pantetheine-free mutants of the yeast fatty-acid-synthetase complex". Eur. J. Biochem. 39 (2): 353–62. doi:10.1111/j.1432-1033.1973.tb03133.x. PMID 4590449. 
• Wakil SJ, Stoops JK, Joshi VC (1983). "Fatty acid synthesis and its regulation". Annu. Rev. Biochem. 52: 537–79. doi:10.1146/annurev.bi.52.070183.002541. PMID 6137188. 

See also

• Long fatty acyl-CoA syntetase