Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Bacillus subtilis |
fabL in pET15b for his-tagged overexpression | Bacillus subtilis |
Protein Variants | Comment | Organism |
---|---|---|
additional information | the ygaA knockout is 250fold more sensitive to the inhibitor triclosan | Bacillus subtilis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
triclosan | half-maximal inhibition at 0.016 mM; reversible inhibitor that does not form a ternary complex; reversibly inhibited by, does not form the stable ternary complex characteristic of the FabI proteins. Expression of YgaA complements the fabI(ts) defect in Escherichia coli and conferrs complete triclosan resistance | Bacillus subtilis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.016 | - |
NADPH | - |
Bacillus subtilis | |
0.016 | - |
NADPH | no cooperativity in binding NADPH | Bacillus subtilis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Bacillus subtilis | part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters | ? | - |
? | |
additional information | Bacillus subtilis | catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein | ? | - |
? | |
additional information | Bacillus subtilis 168 | catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
as there is no information concerning the stereochemistry of hydrogen transfer from NADPH to substrate an appointment to EC 1.3.1.10 or EC 1.3.1.39 is impossible | - |
Bacillus subtilis | P71079 | - |
- |
Purification (Comment) | Organism |
---|---|
Ni2+ affinity chromatography on his-tagged protein | Bacillus subtilis |
Ni2+ chelation chromatography | Bacillus subtilis |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.18 | - |
with octenyl-N-acetyl-cysteamine | Bacillus subtilis |
0.18 | - |
spectrophotometric assay, S-((2E)-oct-2-enoyl)-N-acetylcysteamine as a substrate | Bacillus subtilis |
0.3 | - |
with crotonyl-[acyl-carrier-protein] | Bacillus subtilis |
0.3 | - |
spectrophotometric assay, (2E)-but-2-enoyl-[acyl carrier protein] as a substrate | Bacillus subtilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(2E)-but-2-enoyl-[acyl carrier protein] + NADPH + H+ | - |
Bacillus subtilis | butanoyl-[acyl-carrier protein] + NADP+ | - |
? | |
(2E)-but-2-enoyl-[acyl carrier protein] + NADPH + H+ | - |
Bacillus subtilis 168 | butanoyl-[acyl-carrier protein] + NADP+ | - |
? | |
crotonyl-[acyl-carrier protein] + NADPH | - |
Bacillus subtilis | butyryl-[acyl-carrier protein] + NADP+ | - |
? | |
additional information | part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters | Bacillus subtilis | ? | - |
? | |
additional information | catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein | Bacillus subtilis | ? | - |
? | |
additional information | catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein | Bacillus subtilis 168 | ? | - |
? | |
octenoyl-N-acetyl-cysteamine + NADPH | - |
Bacillus subtilis | octanoyl-N-acetyl-cysteamine + NADP+ | - |
? | |
S-((2E)-oct-2-enoyl)-N-acetylcysteamine + NADPH + H+ | - |
Bacillus subtilis | S-octanoyl-N-acetylcysteamine + NADP+ | - |
? | |
S-((2E)-oct-2-enoyl)-N-acetylcysteamine + NADPH + H+ | - |
Bacillus subtilis 168 | S-octanoyl-N-acetylcysteamine + NADP+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
enoyl-ACP reductase | - |
Bacillus subtilis |
FabL | - |
Bacillus subtilis |
YgaA | - |
Bacillus subtilis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Bacillus subtilis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADPH | inactive with NADH | Bacillus subtilis |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.016 | - |
- |
Bacillus subtilis | triclosan |
General Information | Comment | Organism |
---|---|---|
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 | Bacillus subtilis |