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1.3.1.104
metabolism
the whole reaction involves the formation of the covalent ene adduct and the proton transfer from Tyr79 to the substrate. In the first step the hydride of NADPH easily transfers to crotonyl-CoA to generate the substrate carbanion if the hydroxyl of Tyr79 forms a hydrogen bond chain with Ser70 and crystal water molecules. Then, the carbanion and NADP+ form a stable covalent ene adduct. The formation of the ene adduct follows the Michael addition mechanism rather than the electrocyclic ene reactions. The final electrophilic attack of the Tyr79 proton on C8 of the substrate affords the product of acyl thioester. The key crystal water molecules do not directly participate in the catalytic reactions, but they play a role in maintaining the relative stability of the substrate to NADPH
763551
1.3.1.104
physiological function
expression complements the Escherichia coli fabI temperature-sensitive mutant
390504
1.3.1.104
physiological function
expression of isoform FabL complements the temperature-sensitive fabI defect in Escherichia coli and confers complete triclosan resistance. Knockouts of the FabL gene in Bacillus subtilis are viable, but double knockouts of isoforms FabI and FabL are not obtained. The ygaA knockout is 250fold more sensitive to triclosan than wild-type
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390505
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