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Literature summary 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

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.17.1.4 additional information no substrate inhibition Rhodobacter capsulatus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.17.1.4 0.064
-
 xanthine wild-type, pH 7.8, 25°C Rhodobacter capsulatus
1.17.1.4 0.103
-
 NAD+ wild-type, pH 7.8, 25°C Rhodobacter capsulatus
1.17.1.4 0.163
-
 xanthine mutant E232A, pH 7.8, 25°C Rhodobacter capsulatus

Organism

EC Number Organism UniProt Comment Textmining
1.17.1.4 Rhodobacter capsulatus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.17.1.4
-
 Rhodobacter capsulatus

Substrates and Products (Substrate)

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.17.1.4 4.4
-
 xanthine mutant E232A, pH 7.8, 25°C Rhodobacter capsulatus
1.17.1.4 108
-
 xanthine wild-type, pH 7.8, 25°C Rhodobacter capsulatus