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Literature summary extracted from

  • Mande, S.S.; Parsonage, D.; Claiborne, A.; Hol, W.G.J.
    Crystallographic analyses of NADH peroxidase Cys42Ala and Cys42Ser mutants: active site structures, mechanistic implications, and an unusual environment of Arg303 (1995), Biochemistry, 34, 6985-6992.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.1
-
 Enterococcus faecalis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.11.1.1 hanging drop vapor diffusion method Enterococcus faecalis

Protein Variants

EC Number Protein Variants Comment Organism
1.11.1.1 C42A tertial structure very similar to wild type enzyme Enterococcus faecalis
1.11.1.1 C42S tertial structure very similar to wild type enzyme Enterococcus faecalis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.11.1.1 201400
-
 gel filtration Enterococcus faecalis

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.1 Enterococcus faecalis
-
 Enterococcus faecalis, wild type and mutants
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.1
-
 Enterococcus faecalis

Subunits

EC Number Subunits Comment Organism
1.11.1.1 tetramer wild type, C42A and C42S mutants are tetramers, concluded from crystal structure Enterococcus faecalis

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.1 FAD
-
 Enterococcus faecalis