A3352
Acyl-coenzyme A Synthetase from Pseudomonas sp.
≥2 units/mg protein
Synonym(s):
Acid: CoA ligase (AMP-forming)
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General description
Acyl-coenzyme A synthetase belongs to adenylate-forming enzymes superfamily. It has a conserved adenosine triphosphate/adenosine monophosphate (ATP/AMP) binding motif.
Application
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 .
Biochem/physiol Actions
Acyl coenzyme A synthetase proteins are involved in regulating and facilitating long-chain fatty acid transport in mammalian cells .
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.
Unit Definition
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.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Peroxisomes, classical compartments of eucaryotic cells have significant functions in cellular metabolism, which beta-oxidation fatty acids and detoxification of H2O2 are the most important biochemical process. Defects in genes encoding for peroxisomal proteins result in biochemical malfunctioning of these organelles
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Metazoan internal organs are assembled from polarized tubular epithelia that must set aside an apical membrane domain as a lumenal surface. In a global Caenorhabditis elegans tubulogenesis screen, interference with several distinct fatty-acid-biosynthetic enzymes transformed a contiguous central intestinal lumen
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