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Merck
CN

B1508

Sigma-Aldrich

丁酰辅酶A 锂盐 水合物

≥90%

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别名:
丁酰基辅酶 a 锂盐水合物
经验公式(希尔记法):
C25H42N7O17P3S · xLi+ · yH2O
分子量:
837.62 (free acid basis)
MDL编号:
UNSPSC代码:
41106305
PubChem化学物质编号:
NACRES:
NA.51

质量水平

检测方案

≥90%

形式

powder

储存温度

−20°C

SMILES字符串

[Li+].[Li+].[Li+].[Li+].CCCC(=O)Nc1ncnc2n(cnc12)[C@@H]3O[C@H](COP([O-])(=O)OP([O-])(=O)OCC(C)(C)C(O)C(=O)NCCC(=O)NCCS)[C@@H](OP([O-])([O-])=O)[C@H]3O

InChI

1S/C25H42N7O17P3S.4Li/c1-4-5-16(34)31-21-17-22(29-12-28-21)32(13-30-17)24-18(35)19(48-50(38,39)40)14(47-24)10-45-51(41,42)49-52(43,44)46-11-25(2,3)20(36)23(37)27-7-6-15(33)26-8-9-53;;;;/h12-14,18-20,24,35-36,53H,4-11H2,1-3H3,(H,26,33)(H,27,37)(H,41,42)(H,43,44)(H2,38,39,40)(H,28,29,31,34);;;;/q;4*+1/p-4/t14-,18-,19-,20?,24-;;;;/m1..../s1

InChI key

FKMUWGIOOMBTED-VLFKLNKMSA-J

应用

丁酰 CoA 是丁酰 CoA 脱氢酶的底物。丁酰 CoA 参与脂类和丁酸盐的代谢。丁酰 CoA 可用作多种脂肪酶的底物和 4-羟基丁酸辅酶 a 转移酶的替代底物。丁酰 CoA 或可用于研究新发现的丁酰化翻译后组蛋白修饰过程。

生化/生理作用

丁酰 CoA 是丁酰 CoA 脱氢酶的底物。丁酰 CoA 参与脂类和丁酸盐的代谢。

象形图

Exclamation mark

警示用语:

Warning

危险声明

危险分类

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

靶器官

Respiratory system

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

dust mask type N95 (US), Eyeshields, Gloves


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C Biben et al.
Molecular and cellular biology, 14(5), 3504-3513 (1994-05-01)
A DNase I-hypersensitive site analysis of the 5'-flanking region of the mouse alpha-cardiac actin gene with muscle cell lines derived from C3H mice shows the presence of two such sites, at about -5 and -7 kb. When tested for activity
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Clostridium aminobutyricum ferments 4-aminobutyrate (γ-aminobutyrate, GABA) to ammonia, acetate and butyrate via 4-hydroxybutyrate that is activated to the CoA-thioester catalyzed by 4-hydroxybutyrate CoA-transferase. Then, 4-hydroxybutyryl-CoA is dehydrated to crotonyl-CoA, which disproportionates to butyryl-CoA and acetyl-CoA. Cocrystallization of the CoA-transferase with
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The positively charged lysine residue plays an important role in protein folding and functions. Neutralization of the charge often has a profound impact on the substrate proteins. Accordingly all the known post-translational modifications at lysine have pivotal roles in cell
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Recombinant Candida rugosa lipase 5 (LIP5) has been functionally expressed along with other isoforms in our laboratory. However, the characterization and codon optimization of LIP5 have not been done. In this work, we characterized, codon-optimized and compared LIP5 with commercial
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Gcn5 is a conserved acetyltransferase that regulates transcription by acetylating the N-terminal tails of histones. Motivated by recent studies identifying a chemically diverse array of lysine acyl modifications in vivo, the acyl-chain specificity of the acetyltransferase human Gcn5 (Gcn5L2) was

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