1996年11月1日 · The ability of FabA and FabZ to function in the initial cycle of fatty acid synthesis was determined in assays containing a combination of the FabD, FabH, and FabG enzymes, ACP, NADH, and NADPH as cofactors, and acetyl-CoA plus [2-14 C]malonyl-CoA as substrates to produce β-hydroxy[14 C]butyryl-ACP as described under “Experimental Procedures.”

1996年11月1日 · There are two genes, fabA and fabZ, encoding beta-hydroxyacyl-acyl carrier protein (ACP) dehydratases that function in the dissociated, type II fatty acid synthase system of Escherichia coli. We have investigated their roles in fatty acid synthesis by purifying the two proteins and reconstituting cy …

2015年11月19日 · In Escherichia coli, the acyl carrier protein (AcpP) plays a central role by sequestering and shuttling the growing acyl chain between fatty acid biosynthetic enzymes. FabA, a β-hydroxyacyl-AcpP dehydratase, is an important enzyme in controlling fatty acid chain length and saturation levels.

High-throughput screening of the PaFabA enzyme has discovered a new inhibitor, N42FTA, the first non-suicide inhibitor of this important and attractive target. We further demonstrate that N42FTA inhibits the functional crosslinking assay of AcpP with FabA, indicating that it blocks the native ACP substrate–enzyme complex formation.

The fabA gene of Escherichia coli encodes 3-hydroxydecanoyl-acyl carrier protein (ACP) 2 dehydratase/isomerase, a bifunctional enzyme that introduces the unsaturated fatty acid (UFA) double bond at the C10 level (1–3) (see Fig. 1). As expected fabA mutants require supplementation with UFA for growth .

尽管大肠杆菌的不饱和脂肪酸（UFA）合成途径是此类途径的原型，但多年来积累了一些未解决的问题。关键的参与者是 fabA 和 fabB 基因。早期对 fabA 转录的研究表明，该基因是从两个启动子转录的，其中一个启动子受到 FadR 蛋白的正向调控。

FabA, a β-hydroxyacyl-AcpP dehydratase, is an important enzyme in controlling fatty acid chain length and saturation levels. FabA-AcpP interactions are transient in nature and thus difficult to visualize.

The fabA gene of Escherichia coli encodes beta-hydroxydecanoyl thioester dehydrase (HDDase), a pivotal enzyme in the biosynthesis of the unsaturated fatty acid cis-vaccenic acid, through the anaerobic pathway. This enzyme is specific to bacterial fatty …

The FabA reaction mechanism has been characterized extensively and is best known for its unique ability to isomerize trans-2-decenoyl-ACP to cis-3-decenoyl-ACP, thus initiating unsaturated fatty acid biosynthesis (3, 4, 5, 6, 7, 8, 9, 10, 11, 12). The sequence of the fabA gene is known, and the active site histidine (His-70) has been identified .

2009年6月4日 · Using this system we showed (as has long been known) that FabA is a bifunctional enzyme that catalyzes both the dehydration of 3-hydroxydecanoyl-ACP and well as the reversible isomerization of trans-2-decenoyl-ACP to cis-3- decenoyl-ACP (Fig. 7).