Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.11.1.26 extracted from

  • Nartey, W.; Basak, S.; Kamariah, N.; Manimekalai, M.S.; Robson, S.; Wagner, G.; Eisenhaber, B.; Eisenhaber, F.; Gruber, G.
    NMR studies reveal a novel grab and release mechanism for efficient catalysis of the bacterial 2-Cys peroxiredoxin machinery (2015), FEBS J., 282, 4620-4638 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of residues 1-212 of the N-terminal and linker region of EcAhpF in Escherichia coli BL21 (DE3) Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AE08 AND P35340 P0AE08: subunit C (ahpC), P35340: subunit F (ahpF)
-
Escherichia coli K12 P0AE08 AND P35340 P0AE08: subunit C (ahpC), P35340: subunit F (ahpF)
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
NADH + ROOH + H+ = NAD+ + H2O + ROH proposed mechanism of H2O2 reduction for the AhpC-AhpF complex. binding mechanism in which the C terminus of AhpC wraps around the N-terminal domain, slowing the dissociation rate for an efficient electron transfer process, and a release mechanism mediated by the conformational change of the C terminus of AhpC upon reduction Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADH + H2O2 + H+
-
Escherichia coli NAD+ + 2 H2O
-
?
NADH + H2O2 + H+
-
Escherichia coli K12 NAD+ + 2 H2O
-
?