A3352
Acyl-coenzyme A Synthetase from Pseudomonas sp.
≥2 units/mg protein
Sinónimos:
Acid: CoA ligase (AMP-forming)
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About This Item
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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
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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Journal of Molecular Biology, 388(5), 997-1008 (2009)
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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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