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

BRENDA support

Literature summary 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)

EC Number Cloned (Comment) Organism
1.11.1.1
-
 Enterococcus faecalis

Protein Variants

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

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.1 Enterococcus faecalis
-
-
-
1.11.1.1 Enterococcus faecalis 10C1
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.1
-
 Enterococcus faecalis

Substrates and Products (Substrate)

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.11.1.1 0.000167
-
 NADH C42A mutant at pH 7.0 and 25°C Enterococcus faecalis
1.11.1.1 0.0005
-
 NADH C42S mutant at pH 7.0 and 25°C Enterococcus faecalis
1.11.1.1 1.17
-
 NADH wild type enzyme at pH 7.0 and 25°C Enterococcus faecalis