1.17.1.4: xanthine dehydrogenase
This is an abbreviated version!
For detailed information about xanthine dehydrogenase, go to the full flat file.
Word Map on EC 1.17.1.4
-
1.17.1.4
-
uric
-
1.2.1.37
-
1.1.1.204
-
allopurinol
-
environmental protection
-
ureide
-
1.1.3.22
-
medicine
-
1.2.3.1
-
xanthinuria
-
oxypurines
-
butyrophilins
-
synthesis
-
hypouricemic
-
agriculture
-
biotechnology
-
analysis
-
nutrition
-
molecular biology
- 1.17.1.4
-
uric
-
1.2.1.37
-
1.1.1.204
- allopurinol
- environmental protection
-
ureide
-
1.1.3.22
- medicine
-
1.2.3.1
-
xanthinuria
-
oxypurines
-
butyrophilins
- synthesis
-
hypouricemic
- agriculture
- biotechnology
- analysis
- nutrition
- molecular biology
Reaction
Synonyms
AtXDH1, EC 1.1.1.204, EC 1.2.1.37, IAO1, More, NAD-xanthine dehydrogenase, PaoABC, Retinol dehydrogenase, Rosy locus protein, VvXDH, xanthine dehydrogenase, xanthine dehydrogenase-1, xanthine dehydrogenase-2, xanthine dehydrogenase/oxidase, xanthine oxidoreductase, xanthine-NAD oxidoreductase, xanthine/NAD+ oxidoreductase, xanthine:NAD+ oxidoreductase, XDH, XDH/XO, XDH1, XDH2, XdhC, XOR, YagR, YagS, YagT
ECTree
1.17.1.4 xanthine dehydrogenaseAdvanced search results
results (
results (KM Value
KM Value on EC 1.17.1.4 - xanthine dehydrogenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.004
2-amino-4-hydroxypterin
-
pH 7.0, electron acceptor: methylene blue
0.0071
2-amino-4-hydroxypterin
-
pH 8.0, electron acceptor: methylene blue
0.011
2-amino-4-hydroxypterin
-
increased Km in the presence of pyridoxal
1
4-hydroxypyrazolo(3,4-d)pyrimidine
-
electron acceptor: 2,6-dichlorophenolindophenol
0.047 - 0.079
hypoxanthine
-
measured in the pH range from 6 to 8.9, pH-independent Km
0.0052
NAD+
DTT-treated C-terminally truncated enzyme mutant, pH 7.8, 25°C
0.033
NAD+
-
increased Km for mutant G353D, electron acceptor: pterin
0.054
NAD+
-
immobilized enzyme preparation, pH 7.9, pH dependence, minimum Km at pH 8.1, increasing values below and above
0.1
NAD+
coexpression of genes xdhABC, conditions of high aeration, pH 7.8, 25°C
0.113
NAD+
coexpression of genes xdhABC, conditions of low aeration, pH 7.8, 25°C
0.148
NAD+
coexpression of genes xdhAB, conditions of high aeration, pH 7.8, 25°C
0.156
NAD+
coexpression of genes xdhAB, conditions of low aeration, pH 7.8, 25°C
0.048
NADH
-
increased Km for mutant G353D, electron acceptor: 2,6-dichlorophenolindophenol
0.029
xanthine
-
electron acceptors: phenazine methosulfate/cytochrome c
0.035
xanthine
-
immobilized enzyme preparation, pH 7.9, pH dependence, minimum Km at pH 8.1, increasing values below and above
0.066
xanthine
coexpression of genes xdhAB, conditions of high aeration, pH 7.8, 25°C
0.067
xanthine
coexpression of genes xdhAB, conditions of low aeration, pH 7.8, 25°C
0.085
xanthine
coexpression of genes xdhABC, conditions of high aeration, pH 7.8, 25°C
80.09
xanthine
coexpression of genes xdhABC, conditions of low aeration, pH 7.8, 25°C
additional information
?
-
KM (mM) (cyanoacetylhydrazone 2-formylquinoxaline-1,4-dioxide) (pH 7.4, 37°C), wild-type: 0.0582, mutant G47A: 0.06568, mutant N352A: 0.0601, mutant S360P: 0.09353, mutant R427E: 0.02086, mutant D430H: 0.06468, mutant D431A: 0.06129, mutant S1227A: 0.148, mutant K1230A: 0.162
-
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
-
additional information
additional information
-
Km-value is 0.0025 mg/ml xanthine
-
additional information
additional information
-
Km-value is 0.0025 mg/ml xanthine
-
additional information
additional information
-
Km-value is 0.0025 mg/ml xanthine
-
additional information
additional information
-
Km-value is 0.0025 mg/ml xanthine
-
additional information
additional information
-
Km-value is 0.0025 mg/ml xanthine
-
additional information
additional information
-
Km-value is 0.0025 mg/ml xanthine
-
additional information
additional information
-
Km-value is 0.0025 mg/ml xanthine
-
additional information
additional information
-
2-position hydroxylation is crucial for 8-position hydroxylation. Stopped-flow studies indicate that the rate-limiting step of the reductive half-reaction is not electron transfer from the xanthine substrate to the molybdenum center, but product release
-
additional information
additional information
-
kinetics in presence and absence of cellular retinol binding proteins, apo-CRBP and apo-CRABP, overview
-
additional information
additional information
Michaelis-Menten steady-state kinetics, overview
-
additional information
additional information
steady-state kinetics and reductive half-reaction, stopped flow kinetics, kinetic analysis of wild-type and mutant xanthine dehydrogenases, overview. kred, the limiting rate constant for reduction at high [xanthine], is significantly compromised in the mutant variant E232Q, a result that is inconsistent with Glu232 being neutral in the active site of the wild-type enzyme. The ionized Glu232 of wild-type enzyme plays an important role in catalysis by discriminating against the monoanionic form of substrate, effectively increasing the pKa of the substrate by two pH units and ensuring that at physiological pH the neutral form of the substrate predominates in the Michaelis complex. The product release is principally rate-limiting in catalysis. The disparity in rate constants for the chemical step of the reaction and product release is not as great in the bacterial enzyme as compared with the vertebrate forms. The faster turnover observed with the bacterial enzyme isdue to a faster rate constant for product release than is seen with the vertebrate enzyme
-
additional information
additional information
steady-state kinetics of DTT-treated and untreated C-terminally truncated enzyme mutant
-
