Literature summary for 1.11.1.27 extracted from

Rouhier, N.; Jacquot, J.P.
Molecular and catalytic properties of a peroxiredoxin-glutaredoxin hybrid from Neisseria meningitidis (2003), FEBS Lett., 554, 149-153.

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Cloned(Commentary)

Cloned (Comment)	Organism
1. full-length protein with 345 amino acids, 2. a construction which stretches from the N-terminus to the end of the peroxiredoxin domain, contains 165 amino acids, 3. the grx module, that starts with MAQESVA and ends with the C-terminus of the fusion with 77 amino acids overall, expression in Escherichia coli	Neisseria meningitidis

Protein Variants

Protein Variants	Comment	Organism
C185S	inactive mutant enzyme	Neisseria meningitidis

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
soluble	when expressed in Escherichia coli	Neisseria meningitidis	-	-

Organism

Organism	UniProt	Comment	Textmining
Neisseria meningitidis	-	natural hybrid protein which contains both a peroxiredoxin and a glutaredoxin domain	-

Purification (Commentary)

Purification (Comment)	Organism
-	Neisseria meningitidis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
H2O2 + NADPH	reaction is driven by glutathione which is maintained reduced via NADPH and glutathione reductase. Both the peroxiredoxin and glutaredoxin domains are biochemically active in the natural hybrid protein which contains both a peroxiredoxin and a glutaredoxin domain. When expressed separately, the glutaredoxin domain is catalytically active and the peroxiredoxin domain posseses a weak activity when supplemented with expoenous glutaredoxin	Neisseria meningitidis	H2O + NADP+	-	?

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Release 2023.1 (January 2023)