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Literature summary for 1.14.13.39 extracted from

  • Golser, R.; Gorren, A.C.; Mayer, B.; Schmidt, K.
    Functional characterization of Glu298Asp mutant human endothelial nitric oxide synthase purified from a yeast expression system (2003), Nitric Oxide, 8, 7-14.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Calmodulin
-
Homo sapiens
tetrahydrobiopterin
-
Homo sapiens

Application

Application Comment Organism
medicine no evidence for altered enzyme function of mutant E298D that could explain endothelial dysfunction associated with the E298D polymorphism Homo sapiens

Protein Variants

Protein Variants Comment Organism
E298D comparable to wild-type in heme and flavin content, in affinity to calmodulin and dimerization Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0044
-
L-arginine wild-type Homo sapiens
0.0052
-
L-arginine mutant E298D Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
expression in Pichia pastoris
-

Source Tissue

Source Tissue Comment Organism Textmining
endothelium
-
Homo sapiens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.142
-
wild-type Homo sapiens
0.159
-
mutant E298D Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
-
Homo sapiens 2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
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