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Literature summary extracted from
- The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis (2000), J. Biol. Chem., 275, 40128-40133.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.3.1.9 | - |
Bacillus subtilis |
| 1.3.1.9 | expression in Escherichia coli | Bacillus subtilis |
| 1.3.1.10 | expression in Escherichia coli | Bacillus subtilis |
| 1.3.1.10 | fabL in pET15b for his-tagged overexpression | Bacillus subtilis |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.3.1.9 | additional information | the fabI knockout is as sensitive as the wild-type strain to the inhibitor triclosan | Bacillus subtilis |
| 1.3.1.10 | additional information | the ygaA knockout is 250fold more sensitive to the inhibitor triclosan | Bacillus subtilis |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.3.1.9 | triclosan | a slow-binding inhibitor of bsFabI and formed a stable bsFabI-NAD+-triclosan ternary complex | Bacillus subtilis |  |
| 1.3.1.9 | [5-chloro-2-(2,4-dichlorophenoxy)phenol] | 50% inhibition at 0.016 mM, builds a stable complex with FabI and NAD+, but inhibition of YgaA is reversible | Bacillus subtilis | |
| 1.3.1.10 | 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 | |
| 1.3.1.104 | triclosan | enzyme is reversibly inhibited by triclosan, but does not form a stable ternary complex | Bacillus subtilis | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.3.1.9 | 0.007 | - |
NADH | - |
Bacillus subtilis | |
| 1.3.1.10 | 0.016 | - |
NADPH | - |
Bacillus subtilis | |
| 1.3.1.10 | 0.016 | - |
NADPH | no cooperativity in binding NADPH | Bacillus subtilis | |
| 1.3.1.104 | 0.016 | - |
NADPH | pH 7.5, 25°C | Bacillus subtilis | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.3.1.9 | additional information | Bacillus subtilis | key enzyme in type II fatty-acid synthases that catalyzes the last step in each elongation cycle | ? | - |
? | |
| 1.3.1.10 | additional information | Bacillus subtilis | part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters | ? | - |
? | |
| 1.3.1.10 | additional information | Bacillus subtilis | catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein | ? | - |
? | |
| 1.3.1.10 | additional information | Bacillus subtilis 168 | catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.3.1.9 | Bacillus subtilis | - |
- |
- |
| 1.3.1.9 | Bacillus subtilis | P54616 | - |
- |
| 1.3.1.10 | 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 | - |
| 1.3.1.10 | Bacillus subtilis | P71079 | - |
- |
| 1.3.1.104 | Bacillus subtilis | P71079 | - |
- |
| 1.3.1.104 | Bacillus subtilis 168 | P71079 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.3.1.9 | Ni2+ chelation chromatography | Bacillus subtilis |
| 1.3.1.9 | two enzymes: FabI and YgaA | Bacillus subtilis |
| 1.3.1.10 | Ni2+ affinity chromatography on his-tagged protein | Bacillus subtilis |
| 1.3.1.10 | Ni2+ chelation chromatography | Bacillus subtilis |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.3.1.9 | 0.14 | - |
FabI protein | Bacillus subtilis |
| 1.3.1.9 | 0.14 | - |
spectrophotometric assay, S-((2E)-oct-2-enoyl)-N-acetylcysteamine as a substrate | Bacillus subtilis |
| 1.3.1.9 | 0.18 | - |
YgaA protein | Bacillus subtilis |
| 1.3.1.9 | 2.3 | - |
spectrophotometric assay, (2E)-but-2-enoyl-[acyl carrier protein] as a substrate | Bacillus subtilis |
| 1.3.1.10 | 0.18 | - |
with octenyl-N-acetyl-cysteamine | Bacillus subtilis |
| 1.3.1.10 | 0.18 | - |
spectrophotometric assay, S-((2E)-oct-2-enoyl)-N-acetylcysteamine as a substrate | Bacillus subtilis |
| 1.3.1.10 | 0.3 | - |
with crotonyl-[acyl-carrier-protein] | Bacillus subtilis |
| 1.3.1.10 | 0.3 | - |
spectrophotometric assay, (2E)-but-2-enoyl-[acyl carrier protein] as a substrate | Bacillus subtilis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.3.1.9 | (2E)-but-2-enoyl-[acyl carrier protein] + NADH + H+ | - |
Bacillus subtilis | butanoyl-[acyl-carrier protein] + NAD+ | - |
? | |
| 1.3.1.9 | crotonoyl-CoA + NADH + H+ | - |
Bacillus subtilis | butyryl-CoA + NAD+ | - |
? | |
| 1.3.1.9 | additional information | key enzyme in type II fatty-acid synthases that catalyzes the last step in each elongation cycle | Bacillus subtilis | ? | - |
? | |
| 1.3.1.9 | S-((2E)-oct-2-enoyl)-N-acetylcysteamine + NADH + H+ | - |
Bacillus subtilis | S-octanoyl-N-acetylcysteamine + NAD+ | - |
? | |
| 1.3.1.10 | (2E)-but-2-enoyl-[acyl carrier protein] + NADPH + H+ | - |
Bacillus subtilis | butanoyl-[acyl-carrier protein] + NADP+ | - |
? | |
| 1.3.1.10 | (2E)-but-2-enoyl-[acyl carrier protein] + NADPH + H+ | - |
Bacillus subtilis 168 | butanoyl-[acyl-carrier protein] + NADP+ | - |
? | |
| 1.3.1.10 | crotonyl-[acyl-carrier protein] + NADPH | - |
Bacillus subtilis | butyryl-[acyl-carrier protein] + NADP+ | - |
? | |
| 1.3.1.10 | additional information | part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters | Bacillus subtilis | ? | - |
? | |
| 1.3.1.10 | additional information | catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein | Bacillus subtilis | ? | - |
? | |
| 1.3.1.10 | additional information | catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein | Bacillus subtilis 168 | ? | - |
? | |
| 1.3.1.10 | octenoyl-N-acetyl-cysteamine + NADPH | - |
Bacillus subtilis | octanoyl-N-acetyl-cysteamine + NADP+ | - |
? | |
| 1.3.1.10 | S-((2E)-oct-2-enoyl)-N-acetylcysteamine + NADPH + H+ | - |
Bacillus subtilis | S-octanoyl-N-acetylcysteamine + NADP+ | - |
? | |
| 1.3.1.10 | S-((2E)-oct-2-enoyl)-N-acetylcysteamine + NADPH + H+ | - |
Bacillus subtilis 168 | S-octanoyl-N-acetylcysteamine + NADP+ | - |
? | |
| 1.3.1.104 | trans-2-octenoyl-N-acetylcysteamine + NADPH + H+ | - |
Bacillus subtilis | octanoyl-N-acetylcysteamine + NADP+ | - |
? | |
| 1.3.1.104 | trans-2-octenoyl-N-acetylcysteamine + NADPH + H+ | - |
Bacillus subtilis 168 | octanoyl-N-acetylcysteamine + NADP+ | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.3.1.9 | bsFabI | - |
Bacillus subtilis |
| 1.3.1.9 | enoyl-ACP reductase | - |
Bacillus subtilis |
| 1.3.1.9 | enoyl-[acyl-carrier-protein] reductase | - |
Bacillus subtilis |
| 1.3.1.9 | FabI | - |
Bacillus subtilis |
| 1.3.1.10 | enoyl-ACP reductase | - |
Bacillus subtilis |
| 1.3.1.10 | FabL | - |
Bacillus subtilis |
| 1.3.1.10 | YgaA | - |
Bacillus subtilis |
| 1.3.1.104 | FabL | - |
Bacillus subtilis |
| 1.3.1.104 | YgaA | - |
Bacillus subtilis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.3.1.9 | 25 | - |
assay at | Bacillus subtilis |
| 1.3.1.10 | 25 | - |
assay at | Bacillus subtilis |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.3.1.9 | NADH | FabI protein | Bacillus subtilis | |
| 1.3.1.9 | NADH | inactive with NADPH | Bacillus subtilis | |
| 1.3.1.9 | NADPH | YgaA protein | Bacillus subtilis | |
| 1.3.1.10 | NADPH | inactive with NADH | Bacillus subtilis | |
| 1.3.1.104 | additional information | no cofactor: NADH | Bacillus subtilis | |
| 1.3.1.104 | NADPH | enzyme does not exhibit cooperative binding of NADPH | Bacillus subtilis | |
IC50 Value
| EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
|---|---|---|---|---|---|---|
| 1.3.1.9 | 0.016 | - |
- |
Bacillus subtilis | triclosan | |
| 1.3.1.10 | 0.016 | - |
- |
Bacillus subtilis | triclosan | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.3.1.9 | 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 |
| 1.3.1.10 | 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 |
| 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 | Bacillus subtilis |
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