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Literature summary for 1.6.2.2 extracted from

  • Percy, M.J.; Crowley, L.J.; Davis, C.A.; McMullin, M.F.; Savage, G.; Hughes, J.; McMahon, C.; Quinn, R.J.; Smith, O.; Barber, M.J.; Lappin, T.R.
    Recessive congenital methaemoglobinaemia: functional characterization of the novel D239G mutation in the NADH-binding lobe of cytochrome b5 reductase (2005), Br. J. Haematol., 129, 847-853.
    View publication on PubMed
Search for more literature for 1.6.2.2

Application

Application Comment Organism
medicine isolation of mutations leading to type I recessive congenital methaemoglobinaemia Homo sapiens

Protein Variants

Protein Variants Comment Organism
A178T natural mutation found in patient with type I recessive congenital methaemoglobinaemia, 16.6% of wild-type enzyme activity Homo sapiens
D239G natural mutation found in patient with type I recessive congenital methaemoglobinaemia, mutation of NADH-binding lobe. Mutant shows decreased specificity for NADH and increased specificity for NADPH, 28.5% of wild-type enzyme activity Homo sapiens
E255- natural mutation found in patient with type I recessive congenital methaemoglobinaemia, mutation of NADH-binding lobe. Mutant retains stoichiometric levels FAD comparable to wild-type Homo sapiens
G291D natural mutation found in patient with type I recessive congenital methaemoglobinaemia, mutation of NADH-binding lobe. Mutant retains stoichiometric levels FAD comparable to wild-type and 35.2% of wild-type enzyme activity Homo sapiens
R159-/D239G natural mutation found in patient with type I recessive congenital methaemoglobinaemia, 40.8% of wild-type enzyme activity Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
 patients with type I recessive congenital methaemoglobinaemia
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricyanide + NADH
-
 Homo sapiens 2 ferrocyanide + NAD+ + H+
-
 ?
NADPH + ferricytochrome b5
-
 Homo sapiens NADP+ + H+ + ferrocytochrome b5
-
 r

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3
-
 NADPH mutant E255-, pH 7.0 Homo sapiens
19
-
 NADPH mutant G291D, pH 7.0 Homo sapiens
33
-
 NADPH wild-type, pH 7.0 Homo sapiens
190
-
 NADPH mutant D239G, pH 7.0 Homo sapiens
754
-
 NADH wild-type, pH 7.0 Homo sapiens
754
-
 NADH mutant D239G, pH 7.0 Homo sapiens
754
-
 NADH mutant E255-, pH 7.0 Homo sapiens
754
-
 NADH mutant G291D, pH 7.0 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Homo sapiens
NADPH
-
 Homo sapiens