Acyl-coenzyme A Synthetase from Pseudomonas sp.

Acyl-coenzyme A synthetase belongs to adenylate-forming enzymes superfamily. It has a conserved adenosine triphosphate/adenosine monophosphate (ATP/AMP) binding motif.

Acyl-coenzyme A (coA) synthetase from Pseudomonas sp. has been used:

• as ligase in the synthesis of mevalonate derivatives of adenosine triphosphate (ATP)
• in in vitro fatty acylation assays
• in the synthesis of (¹⁴C)Vernoloyl-CoA (Va-CoA),(3) bisphosphonates derivatives of ATP(4) and (³H)Palmitate-CoA

Acyl-coenzyme A Synthetase may be used to study fatty acid metabolism and lipid metabolism. It has been used to study its interaction with fatty acid transport proteins, which has been found to be involved in the efficient cellular uptake of long-chain fatty acids in adipocytes .

Acyl-coenzyme A (CoA) synthetase (ACS) enzyme catalyzes a two-step thioesterification reaction involving the conversion of free fatty acids (FAs) to CoA esters. The substrate for ACS varies from two carbon to 26 carbon FAs. It is involved in the activation of FAs for lipid metabolism and enables FA to participate in various cellular metabolic pathways.

Acyl coenzyme A synthetase proteins are involved in regulating and facilitating long-chain fatty acid transport in mammalian cells .

One unit will form 1.0 μmole of AMP and oleoyl coenzyme A from ATP and oleate at pH 8.1 at 25 °C in the presence of Coenzyme A.