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Literature summary extracted from

  • Poole, L.B.
    Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their flavoprotein reductases (2005), Arch. Biochem. Biophys., 433, 240-254.
    View publication on PubMed

Crystallization (Commentary)

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

Protein Variants

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

Inhibitors

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

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.8 Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.1.8 25
-
assay at Salmonella enterica subsp. enterica serovar Typhimurium

Cofactor

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