| Identification | Back Directory | [Name]
ACYL-COENZYME A SYNTHETASE | [CAS]
9013-18-7 | [Synonyms]
C:C&B6
EC 6.2.1.3
Acyl-CoA ligase
Acyl-CoA synthase
Acy-CoA Synthelase
Acyl-CoA Synthetase
Fatty acid CoA ligase
Fatty acid thiokinase
Fatty acyl-CoA ligase
Acyl-coenzyme A ligase
Hexanoyl-CoA synthetase
Acyl-CoA synthetase （ACS）
Fatty acyl CoA synthetase
3-Hydroxyacyl-CoA synthase
ACYL-COENZYME A SYNTHETASE
Synthetase, acyl coenzyme A
acetyl coenzyme A synthetase
ACID: COA LIGASE (AMP-FORMING)
Hexanoyl coenzyme A synthetase
Fatty acyl-coenzyme A synthetase
Acyl-CoA synthetase, recombinant
Fatty acid thiokinase (long chain)
Acyl-CoA Synthetase, ≥8U/mg protein
ACYL-COENZYME A SYNTHETASE USP/EP/BP
Acyl-CoA Synthetase / Acid:CoA ligase
Acyl-CoA synthetase from Microorganism
Acyl-coenzyme A Synthetase [>=8 units/mg]
Native Pseudomonas fragi Acyl-CoA Synthetase
acyl-coenzyme a synthetase from pseudomonas sp.
Native Pseudomonas sp. Acyl-coenzyme A Synthetase
ACYL-COENZYME A SYNTHETASE FROM PSEUDO-M ONAS SP., ~2.5U/MG | [EINECS(EC#)]
232-747-5 | [MDL Number]
MFCD00130343 |
| Hazard Information | Back Directory | [Chemical Properties]
White powder | [Uses]
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
| [General Description]
Acyl-coenzyme A synthetase belongs to adenylate-forming enzymes superfamily. It has a conserved adenosine triphosphate/adenosine monophosphate (ATP/AMP) binding motif. | [Biochem/physiol Actions]
Acyl coenzyme A synthetase proteins are involved in regulating and facilitating long-chain fatty acid transport in mammalian cells . | [Purification Methods]
Purify the synthase by extraction with sucrose/HCO3 buffer, protamine sulfate precipitation, (NH4)2SO4 (66-65%) fractination (pH 4.35) and a second (NH4)2SO4 (35-60%) fractionation (pH 4.35). It has Km 0.15mM (Vrel 1.0) for octanoate and 0.41mM (Vrel 2.37) for heptanoate. The Km for ATP is 0.5mM, all at pH 9.0 in ethylene glycol buffer at 38o. [Jencks et al. J Biol Chem 204 453 1953, Methods Enzymol 5 467 1962.] |
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