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Literature summary for 1.7.2.1 extracted from

  • Wijma, H.J.; Macpherson, I.; Alexandre, M.; Diederix, R.E.; Canters, G.W.; Murphy, M.E.; Verbeet, M.P.
    A rearranging ligand enables allosteric control of catalytic activity in copper-containing nitrite reductase (2006), J. Mol. Biol., 358, 1081-1093.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor-diffusion method, mutant enzyme M150G Alcaligenes faecalis

Protein Variants

Protein Variants Comment Organism
M150G mutant enzyme shows lower catalytic activity than the wild-type enzyme. The type-1 site optical spectrum differs significantly from that of the native enzyme. The midpoint potential of the type-1 site of nitrite reductase M150G is higher than that of the native enzyme Alcaligenes faecalis
M150H mutant enzyme shows very low catalytic activity Alcaligenes faecalis
M150T mutant enzyme shows lower catalytic activity than the wild-type enzyme Alcaligenes faecalis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.099
-
nitrite mutant enzyme M150H Alcaligenes faecalis
126
-
nitrite mutant enzyme M150T Alcaligenes faecalis
133
-
nitrite mutant enzyme M150G Alcaligenes faecalis
416
-
nitrite wild-type enzyme Alcaligenes faecalis

Organism

Organism UniProt Comment Textmining
Alcaligenes faecalis P38501
-
-
Alcaligenes faecalis S-6 P38501
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nitrite + reduced pseudoazurin
-
Alcaligenes faecalis NO + oxidized pseudoazurin
-
?
nitrite + reduced pseudoazurin
-
Alcaligenes faecalis S-6 NO + oxidized pseudoazurin
-
?