ACYL-COENZYME A SYNTHETASE CAS 9013-18-7

Introduction：Basic information about ACYL-COENZYME A SYNTHETASE CAS 9013-18-7, including its chemical name, molecular formula, synonyms, physicochemical properties, and safety information, etc.

ACYL-COENZYME A SYNTHETASE Basic information

• Product Name: ACYL-COENZYME A SYNTHETASE
• Synonyms: EC 6.2.1.3;ACID: COA LIGASE (AMP-FORMING);ACYL-COENZYME A SYNTHETASE;Synthetase, acyl coenzyme A;ACYL-COENZYME A SYNTHETASE FROM PSEUDO-M ONAS SP., ~2.5U/MG;acyl-coenzyme a synthetase from pseudomonas sp.;Acyl-coenzyme A Synthetase [>=8 units/mg];Acyl-CoA Synthetase
• CAS: 9013-18-7
• MW: 0
• EINECS: 232-747-5
• Mol File: Mol File

ACYL-COENZYME A SYNTHETASE Chemical Properties

• storage temp.: -20°C
• form: powder
• color: white
• Specific Activity: ≥2units/mg protein

Safety Information

• Safety Statements: 24/25
• WGK Germany: 3
• F: 10
• HS Code: 35079090
• Storage Class: 11 - Combustible Solids

ACYL-COENZYME A SYNTHETASE Usage And Synthesis

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.]