EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.8.1.8 | analysis of the X-ray structure at 2.0 A resolution | Salmonella enterica subsp. enterica serovar Typhimurium |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.8.1.8 | additional information | enzyme is inhibited by mutation of either pair of Cys residues, i.e. Cys129-Cys132, or Cys345-Cys348, construction and functional analysis of a chimeric mutant enzyme comprising the enzymes N-terminal domain attached to the N-terminus of thioredoxin reductase from Escherichia coli, the chimeric mutant can reduce thioredoxin, which the wild-type AhpF is not capable of, overview | Salmonella enterica subsp. enterica serovar Typhimurium |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.8.1.8 | additional information | enzyme is inhibited by alkylation of either pair of Cys residues, i.e. Cys129-Cys132, or Cys345-Cys348 | Salmonella enterica subsp. enterica serovar Typhimurium |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.8.1.8 | additional information | Salmonella enterica subsp. enterica serovar Typhimurium | the disulfide reductase system varies with the organism, overview | ? | - |
? | |
1.8.1.8 | peroxiredoxin disulfide + NADH | Salmonella enterica subsp. enterica serovar Typhimurium | enzyme recycles peroxiredoxin AhpC, enzyme acts in a catalytic cycle reaction together with peroxidase forming the bacterial alkyl hydroperoxide reductase system, formerly known as F-52a | reduced peroxiredoxin + NAD+ | - |
ir |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.8.1.8 | Salmonella enterica subsp. enterica serovar Typhimurium | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.8.1.8 | DTNB + NAD(P)H | - |
Salmonella enterica subsp. enterica serovar Typhimurium | 5-mercapto-2-nitrobenzoate + NAD(P)+ | - |
? | |
1.8.1.8 | additional information | the disulfide reductase system varies with the organism, overview | Salmonella enterica subsp. enterica serovar Typhimurium | ? | - |
? | |
1.8.1.8 | additional information | enzyme contains the CXXCD motif required in thioredoxin reductase for the dithiol-disulfide interchange reaction with thioredoxin corresponding to Cys345 and Cys348 in the enzyme, the enzyme is a thioredoxin reductase-like flavoprotein disulfide reductase, AhpF utilizes the CXXCD motif domain for electron shuttling to AhpC substrate, activity requires conformational changes, catalytic cycle, overview | Salmonella enterica subsp. enterica serovar Typhimurium | ? | - |
? | |
1.8.1.8 | peroxiredoxin disulfide + NAD(P)H | - |
Salmonella enterica subsp. enterica serovar Typhimurium | reduced peroxiredoxin + NAD(P)+ | - |
ir | |
1.8.1.8 | peroxiredoxin disulfide + NADH | enzyme recycles peroxiredoxin AhpC, enzyme acts in a catalytic cycle reaction together with peroxidase forming the bacterial alkyl hydroperoxide reductase system, formerly known as F-52a | Salmonella enterica subsp. enterica serovar Typhimurium | reduced peroxiredoxin + NAD+ | - |
ir |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.8.1.8 | More | the redox-active disulfide in the N-terminal domain, Cys129-Cys132, of the enzyme is in functional communication with the thioredoxin reductase-like disulfide center in the C-terminal portion, Cys345-Cys348, and with FAD | Salmonella enterica subsp. enterica serovar Typhimurium |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.8.1.8 | AhpF | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
1.8.1.8 | disulfide reductase | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.8.1.8 | 25 | - |
assay at | Salmonella enterica subsp. enterica serovar Typhimurium |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.8.1.8 | FAD | binding domain structure, residues 210-327 and 450-521, flavoenzyme, the redox-active disulfide in the N-terminal domain, Cys129-Cys132, of the enzyme is in functional communication with the thioredoxin reductase-like disulfide center in the C-terminal portion, Cys345-Cys348, and with FAD | Salmonella enterica subsp. enterica serovar Typhimurium | |
1.8.1.8 | NAD(P)H | NADH/SS binding domain structure, residues 328-449, physiological reductant is NADH, NADH is strongly favoured over NADPH | Salmonella enterica subsp. enterica serovar Typhimurium |