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Literature summary extracted from

  • Pauff, J.M.; Hemann, C.F.; Juenemann, N.; Leimkuehler, S.; Hille, R.
    The role of arginine 310 in catalysis and substrate specificity in xanthine dehydrogenase from Rhodobacter capsulatus (2007), J. Biol. Chem., 282, 12785-12790.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.17.1.4 R310K absorption spectra similar to wild-type. 20fold decrease of kred-value Rhodobacter capsulatus
1.17.1.4 R310K kred, the limiting rate of enzyme reduction by substrate at high substrate concentration is 20-fold decreased Rhodobacter capsulatus
1.17.1.4 R310M absorption spectra similar to wild-type. 20000fold decrease of kred-value Rhodobacter capsulatus
1.17.1.4 R310M kred, the limiting rate of enzyme reduction by substrate at high substrate concentration is 20000-fold decreased Rhodobacter capsulatus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.17.1.4 additional information
-
 additional information rapid reaction kinetic parameters for substrates xanthine, 2-thioxanthine, 6-thioxanthine, 1-methylxanthine, 2-hydroxy-6-methylpurine, and 2,6-diaminopurine, in wild-type and mutants R310K and R310M Rhodobacter capsulatus

Organism

EC Number Organism UniProt Comment Textmining
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 1-methylxanthine + NAD+ + H2O 10fold reduced kred-value compared to xanthine Rhodobacter capsulatus 1-methylurate + NADH + H+
-
 ?
1.17.1.4 1-methylxanthine + NAD+ + H2O rather less effective than xanthine as a substrate Rhodobacter capsulatus 1-methylurate + NADH + H+
-
 ?
1.17.1.4 2,6-diaminopurine + NAD+ + H2O poor substrate Rhodobacter capsulatus ? + NADH + H+
-
 ?
1.17.1.4 2-hydroxy-6-methylpurine + NAD+ + H2O poor substrate Rhodobacter capsulatus ? + NADH + H+
-
 ?
1.17.1.4 2-thioxanthine + NAD+ + H2O good substrate Rhodobacter capsulatus 2-thiourate + NADH + H+
-
 ?
1.17.1.4 2-thioxanthine + NAD+ + H2O effective substrate Rhodobacter capsulatus 2-thiourate + NADH + H+
-
 ?
1.17.1.4 6-thioxanthine + NAD+ + H2O good substrate Rhodobacter capsulatus ? + NADH + H+
-
 ?
1.17.1.4 6-thioxanthine + NAD+ + H2O effective substrate Rhodobacter capsulatus 6-thiourate + NADH + H+
-
 ?
1.17.1.4 additional information model in which good substrates are bound correctly in the active site in an orientation that allows Arg310 to stabilize the transition state for the first step of the overall reaction via an electrostatic interaction at the C-6 position, thereby accelerating the reaction rate. Poor substrates bind upside down relative to this correct orientation and are unable to avail themselves of the additional catalytic power provided by Arg310 in wild-type enzyme but are significantly less affected by mutations at this position. Analysis of rapid reaction kinetic parameters Rhodobacter capsulatus ?
-
 ?
1.17.1.4 xanthine + NAD+ + H2O
-
 Rhodobacter capsulatus urate + NADH + H+
-
 ?