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Literature summary for 1.17.1.4 extracted from

  • Leimkuhler, S.; Stockert, A.L.; Igarashi, K.; Nishino, T.; Hille, R.
    The role of active site glutamate residues in catalysis of Rhodobacter capsulatus xanthine dehydrogenase (2004), J. Biol. Chem., 279, 40437-40444.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
E232A decrease in kcat value, increase in KM-value Rhodobacter capsulatus
E730A no enzymic activity Rhodobacter capsulatus
E730D no enzymic activity Rhodobacter capsulatus
E730Q no enzymic activity Rhodobacter capsulatus
E730R no enzymic activity Rhodobacter capsulatus

Inhibitors

Inhibitors Comment Organism Structure
additional information no substrate inhibition Rhodobacter capsulatus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.064
-
xanthine wild-type, pH 7.8, 25°C Rhodobacter capsulatus
0.103
-
NAD+ wild-type, pH 7.8, 25°C Rhodobacter capsulatus
0.163
-
xanthine mutant E232A, pH 7.8, 25°C Rhodobacter capsulatus

Organism

Organism UniProt Comment Textmining
Rhodobacter capsulatus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Rhodobacter capsulatus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
xanthine + NAD+ + H2O
-
Rhodobacter capsulatus urate + NADH
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.4
-
xanthine mutant E232A, pH 7.8, 25°C Rhodobacter capsulatus
108
-
xanthine wild-type, pH 7.8, 25°C Rhodobacter capsulatus