EC Number | Cloned (Comment) | Organism |
---|---|---|
1.3.1.10 | fabI in pUC118 | Escherichia coli |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.3.1.10 | G93S | leads to diazaborine resistance | Salmonella enterica subsp. enterica serovar Typhimurium |
1.3.1.10 | G93S | leads to diazaborine resistance | Escherichia coli |
1.3.1.10 | S241F | leads to temperature sensitive growth and abolished activity | Escherichia coli |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.3.1.9 | 6-methyl-2-(propane-1-sulfonyl)-4a,7a-dihydro-2H-thieno[3,2-d][1,2,3]diazaborinin-1-ol | diazaborine derviative 2b18, 90% loss of NADH-dependent activity, 50% loss of NADPH-dependent activity at 0.52 mM | Escherichia coli | |
1.3.1.9 | palmitoyl-CoA | 50% inhibition at 0.0054 mM, competitive inhibition | Escherichia coli | |
1.3.1.10 | 6-methyl-2-(propane-1-sulfonyl)-4a,7a-dihydro-2H-thieno[3,2-d][1,2,3]diazaborinin-1-ol | diazaborine derivative 2b18, binds only in presence of NADH or NADPH, non-competitive inhibition, 0.2 mM lead to 25% inhibition, 0.52 mM to 50%, 1.56 mM to 80%. Increasing the inhibitor concentrations lead to preference for shorter acyl chain lengths | Escherichia coli | |
1.3.1.10 | palmitoyl-CoA | 0.0016 mM lead to 50% inhibition, 0.002 mM to 60%, 0.005 mM to 20%, 0.01 mM to nearly total inhibition | Escherichia coli |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.3.1.9 | 33000 | - |
monomeric form, SDS-PAGE | Escherichia coli |
1.3.1.10 | 33000 | - |
FabI, SDS-PAGE | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.3.1.10 | additional information | Salmonella enterica subsp. enterica serovar Typhimurium | part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters | ? | - |
? | |
1.3.1.10 | additional information | Escherichia coli | part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.3.1.9 | Escherichia coli | - |
wild type and temperature sensitive mutants | - |
1.3.1.10 | Escherichia coli | - |
- |
- |
1.3.1.10 | Salmonella enterica subsp. enterica serovar Typhimurium | - |
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 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.3.1.9 | - |
Escherichia coli |
1.3.1.10 | in BisTris puffer pH 6.5 in order to retain NADPH dependent activity which is lost at pH 7.5 | Escherichia coli |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.3.1.9 | additional information | - |
specific activities in temperature sensitive mutants | Escherichia coli |
1.3.1.10 | 0.008 | - |
crude cell extract | Escherichia coli |
1.3.1.10 | 0.4 | - |
purified by chromatography on DEAE-cellulose and Blue sepharose | Escherichia coli |
EC Number | Storage Stability | Organism |
---|---|---|
1.3.1.10 | -20°C, rapidly inactivated | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.3.1.9 | additional information | enzyme uses as well NADH as NADPH | Escherichia coli | ? | - |
? | |
1.3.1.10 | additional information | part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters | Salmonella enterica subsp. enterica serovar Typhimurium | ? | - |
? | |
1.3.1.10 | additional information | part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters | Escherichia coli | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.3.1.10 | More | NADPH dependent acyl-ACP reductase and NADH dependent acyl-ACP/acyl-CoA reductase activity reside on the same protein | Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.3.1.9 | NADH | - |
Escherichia coli | |
1.3.1.9 | NADPH | - |
Escherichia coli | |
1.3.1.10 | additional information | enzyme also exhibits NADPH dependent activity, if isolated at pH 6.5 | Escherichia coli |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.3.1.9 | 0.02 | - |
palmitoyl-CoA | - |
Escherichia coli |