Yamada J. Long-chain acyl-CoA hydrolase in the brain. Amino Acids. 2005; 28: 273-278. PMID: 15731883Yamada, J. (2005) Long-chain acyl-CoA hydrolase in the brain. Amino Acids 28, 273-278Yamada J. 2005. Long-chain acyl-CoA hydrolase in the brain. Amino Acids 28:273-278....
acyl-CoA hydrolase (CAS 37270-64-7) information, including chemical properties, structure, melting point, boiling point, density, formula, molecular weight, uses, prices, suppliers, SDS and more, available at Chemicalbook.
acyl-coA hydrolase D1 information, including chemical properties, structure, melting point, boiling point, density, formula, molecular weight, uses, prices, suppliers, SDS and more, available at Chemicalbook.
我要写书评 Adp-Dependent Short-Chain-Acyl-Coa Hydrolase的书评 ··· ( 全部0 条 ) 论坛 ··· 在这本书的论坛里发言 + 加入购书单 谁读这本书? ··· 二手市场 ··· 在豆瓣转让 手里有一本闲着? 订阅关于Adp-Dependent Short-Chain-Acyl-Coa Hydrolase的评论: feed: rss 2.0©...
Hepatic enzymes, coash and long-chain acyl-coa in subcellular fractions as affected by drugs inducing peroxisomes and smooth endoplasmic reticulum 1. 1. The activities of acyl-CoA hydrolase, catalase, urate oxidase and peroxisomal palmitoylCoA oxidation as well as the protein content and the level ...
Text A A A A Language: EnglishEspañolDeutschFrançaisItalianoالعربية中文简体PolskiPortuguêsNederlandsNorskΕλληνικήРусскийTürkçeאנגלית Share on FacebookTwitter Get our app Tools A
polifungini was found to be associated with the antibiotic-synthesizing ability, and was negatively correlated with both the thio-esterase activity (acetyl-CoA hydrolase, EC 3.1.2.1) and its affinity towards acetyl-CoA and propionyl-CoA. The apparent Michaelis constants with acetyl-CoA and ...
Long-chain acyl-CoA hydrolase in the brain. Amino Acids 2005; 28: 273–278. 16. Hunt MC, Greene S, Hultenby K, Svensson LT, Engberg S, Alexson SE. Alternative exon usage selectively determines both tissue distribution and subcellular localization of the acyl-CoA thioesterase 7 gene ...
ACOTs are divided into two families, named the Type-I and Type-II thioesterases, where the Type-I thioesterases, together with the acyltransferases, show a high degree of sequence similarity and structurally belong to the α/β-hydrolase superfamily, which is one of the largest superfamilies of...
Palmitic acid could not replace palmitoyl-CoA as the co-substrate indicating that the enzyme involved is an acyl-CoA: ecdysone acyltransferase and not a hydrolase. Formation of ecdysone-palmitate was maximal at 150–200 μM palmitoyl-CoA and was linear with time for up to 1 h. The enzyme ...