The enzyme completes each cycle of fatty acid elongation by catalysing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to the acyl-carrier protein, in an NADPH-dependent manner. This entry stands for enzymes whose stereo-specificity with respect to NADP+ is not known. [cf. EC 1.3.1.39 enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific), EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH)].
Specify your search results
The enzyme appears in viruses and cellular organisms
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
acyl-[acyl-carrier protein]:NADP+ oxidoreductase
The enzyme completes each cycle of fatty acid elongation by catalysing the stereospecific reduction of the double bond at position 2 of a growing fatty acid chain, while linked to the acyl-carrier protein, in an NADPH-dependent manner. This entry stands for enzymes whose stereo-specificity with respect to NADP+ is not known. [cf. EC 1.3.1.39 enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific), EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH)].
antibiotic AFN-1252, i.e. (2E)-N-methyl-N-[(3-methyl-1-benzofuran-2-yl)methyl]-3-(7-oxo-5,6,7,8-tetrahydro-1,8-naphthyridin-3-yl)prop-2-enamide, only binds to the NADPH form of FabI
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
both free form and complexed with NADP+ and inhibitor triclosan, to 2.2 and 1.8 A resolution, respectively. The substrate-binding region in the apo-FabL structure is found in the open form. In addition, the beta4-alpha5 and beta5-alpha7 regions, which include the catalytic residues as well as the cofactor binding residues, get collapsed into the pocket. These differences result in a tetrameric arrangement totally different from NADH-dependent isoform FabI
mutant is resistant to antibiotic AFN-1252 and to triclosan, about 5% of wild-type catalytic activity. A strain expressing Y147H has a pronounced growth defect that is rescued by exogenous fatty acid supplementation
mutant is resistant to antibiotic AFN-1252 and to triclosan, about 5% of wild-type catalytic activity. A strain expressing Y147H has a pronounced growth defect that is rescued by exogenous fatty acid supplementation
replacement of amino acids 55-66 by CurF enoyl reductase cyclopropanase loop leads to gain-of-function activity as a cyclopropanase. With substrate 3-chloromethyl-crotonyl-[acyl-carrier-protein], the formation of both the reduced product and also the cyclopropanated productis detected at levels of about one-quarter of the total product
mutant is resistant to antibiotic AFN-1252 but susceptible to triclosan. Strains expressing M99T exhibit normal growth, and the biochemical properties of the purified protein are indistinguishable from those of FabI
mutant is resistant to antibiotic AFN-1252 but susceptible to triclosan. Strains expressing M99T exhibit normal growth, and the biochemical properties of the purified protein are indistinguishable from those of FabI
development of a simple thermal shift assay, which does not use ACP-linked substrates, to determine the binding ability of triclosan to the enzyme's active site
development of a simple thermal shift assay, which does not use ACP-linked substrates, to determine the binding ability of triclosan to the enzyme's active site
HOME
login
history
all enzymes
BRENDA home
History
1.3.1.104 enoyl-[acyl-carrier-protein] reductase (NADPH)
more
top
Information
