2003年12月19日 · beta-Ketoacyl-acyl carrier protein (ACP) synthase III (KAS III, also called acetoacetyl-ACP synthase) encoded by the fabH gene is thought to catalyze the first elongation reaction (Claisen condensation) of type II fatty acid synthesis in bacteria and plant plastids.

2003年12月19日 · β-Ketoacyl-acyl carrier protein (ACP) synthase III (KAS III, also called acetoacetyl-ACP synthase) encoded by the fabH gene is thought to catalyze the first elongation reaction (Claisen condensation) of type II fatty acid synthesis in bacteria and plant plastids.

Two genes that were predicted to encode homologs of the β-ketoacyl-acyl carrier protein synthase III of Escherichia coli (eFabH) were identified in the Bacillus subtilis genome. Their protein products were expressed, purified, and biochemically characterized.

2024年1月2日 · 大肠杆菌编码3种3-酮脂酰ACP合成酶Ⅰ (FabB)、Ⅱ (FabF)和Ⅲ (FabH)，其中fabF、fabH位于保守的脂肪酸合成基因簇中，而fabB与fabA独立存在。 FabH催化乙酰CoA与丙二酸单酰ACP聚合，完成脂肪酸合成起始 [ 19 ] 。

2019年6月1日 · The enzyme FabH catalyzes the initial step of fatty acid biosynthesis that is essential for bacterial survival. Therefore, FabH has been identified as an attractive target for the development of new antibacterial agents.

2022年1月14日 · In recent years, β-ketoacyl-acyl carrier protein synthase III (FabH) become an attractive new target, which catalyzes the first step of fatty acid biosynthesis, and FabH inhibitors could be potential candidates for antibacterial agents. In this review, recent advances in the research of FabH inhibitors are reviewed.

FabH酶催化脂肪酸生物合成的第一步，这对于细菌的生存至关重要。 因此，FabH已被确定为开发新型抗菌剂的有吸引力的靶标。 我们在这里提出了一种有前景的，具有低毒性和强效FabH抑制作用的吡唑-苯并咪唑酰胺新系列的发现。

In bacterial type II fatty acid biosynthesis (FAS-II), β-ketoacyl-acyl carrier protein (ACP) synthase III (FabH) initiates the first condensation of acyl-CoA and malonyl-ACP to form acetoacetyl-ACP. Its key role for organism survival and specificity to bacteria make it as an essential target for the …

We report the crystal structures of bacterial FabH enzymes from four different pathogenic species: Enterococcus faecalis, Haemophilus influenzae, Staphylococcus aureus and Escherichia coli. Structural data on the enzyme from different species show important differences in the architecture of the substrate-binding sites that parallel the inter ...

After optimization for Gram-negative enzyme inhibitory potency, several compounds demonstrated antimicrobial activity against an efflux-negative strain of Haemophilus influenzae. Mutants resistant to these compounds had mutations in the FabH gene near the catalytic triad, validating FabH as a target for antimicrobial drug discovery.