Home>>Decanoyl Coenzyme A

Decanoyl Coenzyme A

(Synonyms: 癸酰辅酶A,Decanoyl CoA) 目录号 : GC45751

An acyl-CoA thioester

Decanoyl Coenzyme A Chemical Structure

Cas No.:1264-57-9

规格 价格 库存 购买数量
1mg
¥428.00
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5mg
¥1,936.00
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10mg
¥3,426.00
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产品描述

Decanoyl coenzyme A (CoA) is a thioester of decanoic acid and CoA .1 It inhibits the activity of citrate synthase (CS) and glutamate dehydrogenase (GDH) in mitochondria isolated from rat brain (IC50s = 437 and 420 μM, respectively).2 Decanoyl CoA also binds the fatty acid metabolism regulator protein (FadR) promoter in E. coli (Ki = 2 μM).3 It is produced during isomerase-dependent β-oxidation of oleic acid in isolated rat heart mitochondria.4

|1. Gregersen, N., K•lvraa, S., and Mortensen, P.B. Acyl-CoA: Glycine N-acyltransferase: In vitro studies on the glycine conjugation of straight- and branched-chained acyl-CoA esters in human liver. Biochem. Med. Metab. Biol. 35(2), 210-218 (1986).|2. Lai, J.C., Lian, B.B., Zhai, S., et al. Brain mitochondrial citrate synthase and glutamate dehydrogenase: Differential inhibition by fatty acyl coenzyme A derivatives. Metab. Brain Dis. 9(2), 143-152 (1994).|3. DiRusso, C.C., Heimert, T.L., and Metzger, A.K. Characterization of FadR, a global transcriptional regulator of fatty acid metabolism in Escherichia coli. Interaction with the fadB promoter is prevented by long chain fatty acyl coenzyme A. J. Biol. Chem. 267(12), 8685-8691 (1992).|4. Ren, Y., and Schulz, H. Metabolic functions of the two pathways of oleate β-oxidation double bond metabolism during the β-oxidation of oleic acid in rat heart mitochondria. J. Biol. Chem. 278(1), 111-116 (2003).

Chemical Properties

Cas No. 1264-57-9 SDF
别名 癸酰辅酶A,Decanoyl CoA
Canonical SMILES O[C@H]1[C@H](N2C=NC3=C2N=CN=C3N)O[C@H](COP(OP(OCC(C)(C)[C@@H](O)C(NCCC(NCCSC(CCCCCCCCC)=O)=O)=O)(O)=O)(O)=O)[C@H]1OP(O)(O)=O
分子式 C31H54N7O17P3S 分子量 921.8
溶解度 Soluble in DMSO 储存条件 Store at -20°C
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溶解性数据

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1 mg 5 mg 10 mg
1 mM 1.0848 mL 5.4242 mL 10.8483 mL
5 mM 0.217 mL 1.0848 mL 2.1697 mL
10 mM 0.1085 mL 0.5424 mL 1.0848 mL
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Research Update

The Vibrio cholerae quorum-sensing autoinducer CAI-1: analysis of the biosynthetic enzyme CqsA

Nat Chem Biol 2009 Dec;5(12):891-5.PMID:19838203DOI:10.1038/nchembio.237.

Vibrio cholerae, the bacterium that causes the disease cholera, controls virulence factor production and biofilm development in response to two extracellular quorum-sensing molecules, called autoinducers. The strongest autoinducer, called CAI-1 (for cholera autoinducer-1), was previously identified as (S)-3-hydroxytridecan-4-one. Biosynthesis of CAI-1 requires the enzyme CqsA. Here, we determine the CqsA reaction mechanism, identify the CqsA substrates as (S)-2-aminobutyrate and Decanoyl Coenzyme A, and demonstrate that the product of the reaction is 3-aminotridecan-4-one, dubbed amino-CAI-1. CqsA produces amino-CAI-1 by a pyridoxal phosphate-dependent acyl-CoA transferase reaction. Amino-CAI-1 is converted to CAI-1 in a subsequent step via a CqsA-independent mechanism. Consistent with this, we find cells release > or =100 times more CAI-1 than amino-CAI-1. Nonetheless, V. cholerae responds to amino-CAI-1 as well as CAI-1, whereas other CAI-1 variants do not elicit a quorum-sensing response. Thus, both CAI-1 and amino-CAI-1 have potential as lead molecules in the development of an anticholera treatment.