ACYL CARRIER PROTEIN FROM ESCHERICHIA-COLI - CHARACTERIZATION BY PROTON AND F-19 NUCLEAR MAGNETIC-RESONANCE AND EVIDENCE FOR RESTRICTED MOBILITY OF FATTY-ACID CHAIN IN TETRADECANOYL-ACYL-CARRIER PROTEIN
ACYL CARRIER PROTEIN FROM ESCHERICHIA-COLI - CHARACTERIZATION BY PROTON AND F-19 NUCLEAR MAGNETIC-RESONANCE AND EVIDENCE FOR RESTRICTED MOBILITY OF FATTY-ACID CHAIN IN TETRADECANOYL-ACYL-CARRIER PROTEIN
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DOI：
10.1021/bi00618a009
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发表时间：
1978-01-01
期刊：
影响因子：
2.9
通讯作者：
CRONAN, JE
中科院分区：
文献类型：
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作者：
GALLY, HU;SPENCER, AK;CRONAN, JE
E.大肠杆菌的蛋白质是具有4“-磷酸泛酰巯基乙胺辅基的MW 8847的蛋白质。ACP（通过辅基的SH）在脂肪酸和复合脂质的合成中作为辅酶发挥作用。本文报道了在不同实验条件下ACP结构的质子核磁共振研究。通过对五氟十四酰基-ACP的19 F NMR研究，研究了酰基-ACP的脂肪酰基链的运动。还报道了ACP和酰基-ACP的辅基P的31 P NMR研究。ACP的结构通过表面电荷而稳定，酰基-ACP的脂肪酸残基不能自由移动，并且似乎通过与蛋白质部分的相互作用而固定。
The acyl-carrier protein (ACP) of E. coli is a protein of MW 8847 with a 4''-phosphopantetheine prosthetic group. ACP functions (via the SH of the prosthetic group) as a coenzyme in the synthesis of fatty acids and complex lipids. Proton NMR studies of the structure of ACP under various experimental conditions were reported. The motion of the fatty acyl chain of acyl-ACP was investigated by 19F NMR studies of fifluorotetradecanoyl-ACP. 31P NMR studies of the prosthetic group P of ACP and acyl-ACP are also reported. The structure of ACP is stabilized by surface charge, and the fatty acid residue of acyl-ACP does not move freely and seems immobilized by an interaction with the protein moiety.