Cloned (Comment) | Organism |
---|---|
fabI of strain RN4220 found by homology and cloned into pET15b for his-tagged overexpression | Staphylococcus aureus |
Protein Variants | Comment | Organism |
---|---|---|
G93V | leads to triclosan resistance | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Hexachlorophene | half-maximal inhibition at 0.004 mM | Staphylococcus aureus | |
triclosan | half-maximal inhibition at 0.003 mM; slow-binding inhibitor forms a stable, ternary complex with enzyme and NADP+ | Staphylococcus aureus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
NADPH | value above 2 mM | Escherichia coli | |
additional information | - |
NADPH | half-maximal rate at 0.065 mM NADPH | Staphylococcus aureus | |
additional information | - |
NADPH | cooperative binding with Hill coefficient 2.2 | Staphylococcus aureus | |
8 | - |
Crotonyl-N-acetyl-cysteamine | Vmax 0.0003 nmol/min/mg | Staphylococcus aureus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Escherichia coli | part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters | ? | - |
? | |
additional information | Staphylococcus aureus | part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Staphylococcus aureus | Q9RMI3 | 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 | - |
Purification (Comment) | Organism |
---|---|
Ni2+ affinity chromatography on his-tagged protein | Staphylococcus aureus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
crotonyl-N-acetyl-cysteamine + NADPH | - |
Staphylococcus aureus | butyryl-N-acetyl-cysteamine + NADP+ | - |
? | |
additional information | part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters | Escherichia coli | ? | - |
? | |
additional information | part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters | Staphylococcus aureus | ? | - |
? | |
octenoyl-N-acetyl-cysteamine + NADPH | - |
Staphylococcus aureus | octanoyl-N-acetyl-cysteamine + NADP+ | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | enzyme is highly specific for NADH, even if isolated at pH 6.5 | Escherichia coli |