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

BRENDA support

Literature summary for 1.11.1.1 extracted from

  • Parsonage, D.; Claiborne, A.
    Analysis of the kinetic and redox properties of NADH peroxidase C42S and C42A mutants lacking the cysteine-sulfenic acid redox center (1995), Biochemistry, 34, 435-441.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Enterococcus faecalis

Protein Variants

Protein Variants Comment Organism
C42A mutation leads to an almost inactive enzyme Enterococcus faecalis
C42S mutation leads to an almost inactive enzyme Enterococcus faecalis

Organism

Organism UniProt Comment Textmining
Enterococcus faecalis
-
-
-
Enterococcus faecalis 10C1
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Enterococcus faecalis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADH + H2O2
-
Enterococcus faecalis NAD+ + H2O
-
?
NADH + H2O2
-
Enterococcus faecalis 10C1 NAD+ + H2O
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.000167
-
NADH C42A mutant at pH 7.0 and 25°C Enterococcus faecalis
0.0005
-
NADH C42S mutant at pH 7.0 and 25°C Enterococcus faecalis
1.17
-
NADH wild type enzyme at pH 7.0 and 25°C Enterococcus faecalis