Literature summary for 1.8.1.8 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.

Search for more literature for 1.8.1.8

Crystallization (Commentary)

Crystallization (Comment)	Organism
analysis of the X-ray structure at 2.0 A resolution	Salmonella enterica subsp. enterica serovar Typhimurium

Protein Variants

Protein Variants	Comment	Organism
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

Inhibitors	Comment	Organism	Structure
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)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Salmonella enterica subsp. enterica serovar Typhimurium	the disulfide reductase system varies with the organism, overview	?	-	?
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

Organism	UniProt	Comment	Textmining
Salmonella enterica subsp. enterica serovar Typhimurium	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
DTNB + NAD(P)H	-	Salmonella enterica subsp. enterica serovar Typhimurium	5-mercapto-2-nitrobenzoate + NAD(P)+	-	?
additional information	the disulfide reductase system varies with the organism, overview	Salmonella enterica subsp. enterica serovar Typhimurium	?	-	?
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	?	-	?
peroxiredoxin disulfide + NAD(P)H	-	Salmonella enterica subsp. enterica serovar Typhimurium	reduced peroxiredoxin + NAD(P)+	-	ir
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

Subunits	Comment	Organism
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

Synonyms	Comment	Organism
AhpF	-	Salmonella enterica subsp. enterica serovar Typhimurium
disulfide reductase	-	Salmonella enterica subsp. enterica serovar Typhimurium

Temperature Optimum [°C]

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

Cofactor

Cofactor	Comment	Organism	Structure
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
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

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Release 2023.1 (January 2023)