1MKB
ESCHERICHIA COLI BETA-HYDROXYDECANOYL THIOL ESTER DEHYDRASE AT PH 5 AND 21 DEGREES C
1MKB の概要
| エントリーDOI | 10.2210/pdb1mkb/pdb |
| 分子名称 | BETA-HYDROXYDECANOYL THIOL ESTER DEHYDRASE (2 entities in total) |
| 機能のキーワード | fatty acid biosynthesis |
| 由来する生物種 | Escherichia coli |
| 細胞内の位置 | Cytoplasm: P0A6Q3 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 37719.70 |
| 構造登録者 | |
| 主引用文献 | Leesong, M.,Henderson, B.S.,Gillig, J.R.,Schwab, J.M.,Smith, J.L. Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site. Structure, 4:253-264, 1996 Cited by PubMed Abstract: Escherichia coli beta-hydroxydecanoyl thiol ester dehydrase (dehydrase) is essential to the biosynthesis of unsaturated fatty acids, by shunting a 10-carbon intermediate from the saturated fatty acid pathway into the unsaturated fatty acid pathway. Dehydrase catalyzes reactions of dehydration and of double-bond isomerization on 10-carbon thiol esters of acyl carrier protein (ACP). The aim of this work is to elucidate mechanisms for the two enzymatic reactions, which occur in an unusual bifunctional active site, and to understand the specificity of the enzyme for substrates with 10-carbon fatty acyl chains. PubMed: 8805534DOI: 10.1016/S0969-2126(96)00030-5 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
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