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FabG often substitutes other dehydrogenases for producing secondary metabolites in nature. This redundancy is probably due to gene duplication or addition events possibly making FabG, a progenitor to some of the complex short-chain dehydrogenases used in organisms and industries today.
FabG is a 3-ketoacyl-ACP reductase that catalyzes a key step in fatty acid synthesis. This study shows that FabG mutants lacking the conserved Ser, Tyr, and Lys residues are still active, challenging the classification of FabG as a SDR enzyme.
In enzymology, a 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) is an enzyme that catalyzes the chemical reaction. 3-oxoacyl-[acyl-carrier-protein]() + NADPH + H + (3R)-3-hydroxyacyl-[acyl-carrier-protein]() + NADP +This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group as hydride donor with NAD + or NADP + as hydride acceptor.
Core biochemical pathways such as Fatty-acid synthesis II (FAS II) is ascribed to the synthesis of fatty-acids, biotin and lipoic acid in prokaryotes. It has two dehydrogenases namely, FabG and FabI which interact with the fatty-acid chain bound to Acyl-carrier protein (ACP), a well-studied enzyme which binds to substrates of varying lengths. This protein-protein interaction 'broadens ...
Overall, analysis of the FabG sequence, structure, and enzymatic assays, suggests FabG (ABO11256.2) is indeed a functional, and is likely the primary 3-oxoacyl-ACP reductase of A. baumannii.
The 3-ketoacyl-ACP reductase gene (fabG) is located within the fab gene cluster between the fabD and acpP genes and is co-transcribed with acpP. Insertional mutants that prevent fabG transcription while allowing ACP to be produced were generated in the Cronan laboratory and suggest that fabG-encoded reductase activity is essential in E. coli.
We report that fabG3 expression restored the growth of the Escherichia coli fabG temperature-sensitive mutant CL104 under non-permissive conditions. In vitro assays demonstrated that FabG3 catalyses the reduction of 3-oxoacyl-acyl carrier protein (ACP) intermediates in fatty acid synthetic reactions, although FabG3 had a lower activity than FabG1.
Among these Fab enzymes, 3-oxoacyl acyl carrier protein reductase (also called FabG, encoded by the fabG gene) catalyses the essential 3-oxoacyl reduction step in fatty acid biosynthesis in the presence of NADH or NADPH [13].In addition to its lipogenic role, FabG exhibits other functions involved in biological processes.
FabG achieves allosteric regulation of ACP and NADPH through ACP binding across two adjacent FabG monomers, while FabI follows an irreversible compulsory order of substrate binding in that NADH binding must precede that of ACP on a discrete FabI monomer. Moreover, FabG and FabI utilize a backdoor residue Phe187 or a "rheostat" α8 helix for ...
Codon-optimized fabG was chosen to create a sequence sufficiently distinct from the chromosomal fabG to help prevent possible integration of plasmid sequence into the chromosome via homologous recombination. Each strain reached a final OD 600 of approximately 0.45 after 24 h, and there were no significant differences in growth among the strains ...