1.3.1.9: enoyl-[acyl-carrier-protein] reductase (NADH)
This is an abbreviated version!
For detailed information about enoyl-[acyl-carrier-protein] reductase (NADH), go to the full flat file.
Word Map on EC 1.3.1.9
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1.3.1.9
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tuberculosis
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mycobacterium
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triclosan
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falciparum
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plasmodium
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isoniazid
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medicine
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antitubercular
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mycolic
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antimycobacterial
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diazaborine
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triclosan-resistant
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pyrrolyl
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comsia
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surflex-docking
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inh-resistant
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drug development
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analysis
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pharmacology
- 1.3.1.9
- tuberculosis
- mycobacterium
- triclosan
- falciparum
- plasmodium
- isoniazid
- medicine
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antitubercular
-
mycolic
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antimycobacterial
- diazaborine
-
triclosan-resistant
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pyrrolyl
-
comsia
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surflex-docking
-
inh-resistant
- drug development
- analysis
- pharmacology
Reaction
Synonyms
2-trans enoyl-ACP-reductase, 2-trans enoyl-acyl carrier protein reductase, 2-trans-enoyl-ACP (CoA) reductase, 2-trans-enoyl-ACP reductase, 2-trans-enoyl-ACP(CoA) reductase, ACP reductase, BaENR, BMA0885, bsFabI, cold-shock induced protein 15, CSI15, EACP reductase, enoyl (acyl carrier protein) reductase, enoyl ACP reductase, enoyl acyl carrier protein reductase, enoyl acyl carrier protein reductase InhA, enoyl reductase, enoyl-ACP reductase, enoyl-ACP reductase I, enoyl-ACP reductase III, enoyl-ACP(CoA) reductase, enoyl-acyl carrier protein, enoyl-acyl carrier protein reductase, enoyl-acyl carrier protein reductase I, enoyl-reductase, enoyl-[acyl-carrier-protein] reductase, ENR, ENR1, ENR2, FabI, FabI-1, FabI-related enoyl-ACP reductase, FabI1, FabI2, FabK, Fabl1, Fabl2, FabMG, FabV, FAS-II enoyl reductase, FTT_0782, InhA, More, MtENR, MtInhA, NAD-dependent enoyl-ACP reductase, NADH-dependent enoyl reductase, NADH-dependent enoyl-ACP reductase, NADH-dependent enoyl-acyl carrier protein reductase, NADH-enoyl acyl carrier protein reductase, NADH-ENR, NADH-specific enoyl-ACP reductase, OsmC, PA2950, pfENR, reductase, enoyl-[acyl carrier protein], trans-enoyl-[acyl carrier protein] reductase, trans-enoyl-[acyl-carrier-protein] reductase, VEG241, vegetative protein 241, VF_0888, YP_4011
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General Information on EC 1.3.1.9 - enoyl-[acyl-carrier-protein] reductase (NADH)
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
malfunction
physiological function of the enzyme is examined by knocking out the gene and determining the effect of the gene disruptions on cell growth and triclosan sensitivity, the gene is not essential
metabolism
physiological function
metabolism
enoyl-ACP reductases catalyze the final step in the elongation cycle of the bacterial fatty acid biosynthesis, FAS-II, pathway, but FabV is distinct and belongs to another class of enoyl-acyl carrier protein reductases, overview
metabolism
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the enzyme catalyzes the last step in each elongation cycle of type II bacterial fatty acid synthesis and is a key regulatory protein in bacterial fatty acid synthesis
metabolism
the enzyme catalyzes the NADH-dependent reduction of long-chain trans-2-enoyl-ACP fatty acids, an intermediate in mycolic acid biosynthesis
metabolism
the enzyme is a member of the mycobacterial type II dissociated fatty acid biosynthesis system
metabolism
the enzyme is an essential enzyme of the mycolic acid biosynthetic pathway
metabolism
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the enzyme is involved in mycolic acid biosynthesis. It is part of the dissociative type 2 fatty acid synthase (FASII) system
metabolism
the enzyme is involved in the biosynthesis of mycolic acids
metabolism
the enzyme is involved in the type II fatty acid biosynthesis pathway of Mycobacterium tuberculosis
metabolism
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the enzyme is involved on the biosynthetic pathway for mycolic acids
metabolism
the NADH cofactor and the CoA thioester substrate form a covalent adduct during the InhA catalytic cycle. Residue Tyr158 is required for the stereospecificity of protonation and Thr196 is partially involved in hydride transfer and protonation
metabolism
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the enzyme is involved in the synthesis of cell wallmycolic acid
metabolism
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enoyl-ACP reductases catalyze the final step in the elongation cycle of the bacterial fatty acid biosynthesis, FAS-II, pathway, but FabV is distinct and belongs to another class of enoyl-acyl carrier protein reductases, overview
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metabolism
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the enzyme is involved in the synthesis of cell wallmycolic acid
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metabolism
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the NADH cofactor and the CoA thioester substrate form a covalent adduct during the InhA catalytic cycle. Residue Tyr158 is required for the stereospecificity of protonation and Thr196 is partially involved in hydride transfer and protonation
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metabolism
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the enzyme is involved in the type II fatty acid biosynthesis pathway of Mycobacterium tuberculosis
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metabolism
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the enzyme catalyzes the NADH-dependent reduction of long-chain trans-2-enoyl-ACP fatty acids, an intermediate in mycolic acid biosynthesis
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metabolism
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key enzyme in the biosynthesis of mycolic acids
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metabolism
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the enzyme is a member of the mycobacterial type II dissociated fatty acid biosynthesis system
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metabolism
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the enzyme is involved in the biosynthesis of mycolic acids
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metabolism
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the enzyme is an essential enzyme of the mycolic acid biosynthetic pathway
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physiological function
enoyl reductase, ENR, a type II fatty acid synthase enzyme essential in parasites but not present in host animals
physiological function
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PfENR reduces the trans-2 enoyl bond of enoyl-ACP substrates to saturated acyl-ACPs and plays a crucial role in completing the successive rounds of fatty acid elongation
physiological function
expression in Escherichia coli restores growth and the fatty acid synthesis of the Escherichia coli fabl temperature sensitive mutant JP1111 under nonpermissive conditions
physiological function
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fatty acid biosynthesis and FabI activity are essential for growth even in the presence of exogenous long-chain lipids. FabI is not transcriptionally altered in the presence of exogenous long-chain lipids. Inhibition of FabI or fatty acid synthesis results in loss of viability that is not rescued by exogenous long-chain lipid supplementation. FabI and de novo fatty acid biosynthetic genes are transcriptionally active during infection
physiological function
isoform FabV confers triclosan resistance on Pseudomonas aeruginosa. Upon deletion of the fabV gene, the mutant strain becomes more than 2000fold more sensitive to triclosan than the wild-type strain. Enzyme functionally replaces Escherichia coli fabI in vivo and renders Escherichia coli resistant to triclosan
physiological function
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the enzyme is essential for the intracellular growth of Listeria monocytogenes
physiological function
the enzyme is able to complement an Escherichia coli JP1111 FabI mutant strain. When ENR2 is expressed together with FabI the proportion of saturated fatty acids decreases from 50 to 30%
physiological function
the enzyme is able to complement an Escherichia coli JP1111 fabI strain
physiological function
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fatty acid biosynthesis and FabI activity are essential for growth even in the presence of exogenous long-chain lipids. FabI is not transcriptionally altered in the presence of exogenous long-chain lipids. Inhibition of FabI or fatty acid synthesis results in loss of viability that is not rescued by exogenous long-chain lipid supplementation. FabI and de novo fatty acid biosynthetic genes are transcriptionally active during infection
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