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1.17.3.2: xanthine oxidase

This is an abbreviated version!
For detailed information about xanthine oxidase, go to the full flat file.

Word Map on EC 1.17.3.2

Reaction

xanthine
+
H2O
 +
O2
=
Urate
 +
H2O2

Synonyms

AXOR, EC 1.1.3.22, EC 1.2.3.2, EC 1.2.3.2., hypoxanthine oxidase, hypoxanthine-xanthine oxidase, hypoxanthine:oxygen oxidoreductase, More, oxidase, xanthine, Schardinger enzyme, xanthine dehydrogenase/oxidase, xanthine oxidase, xanthine oxidoreductase, xanthine: oxygen oxidoreductase, xanthine:O2 oxidoreductase, xanthine:oxygen oxidoreductase, xanthine:xanthine oxidase, XnOx, XO, XOD, XOR

ECTree

     1 Oxidoreductases
         1.17 Acting on CH or CH2 groups
             1.17.3 With oxygen as acceptor
                1.17.3.2 xanthine oxidase

Engineering

Engineering on EC 1.17.3.2 - xanthine oxidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E1261X
-
mutation of Glu1261 leads to a complete loss of activity
E802Q
-
site-directed mutagenesis, altered kinetics of the mutant enzyme compared to the wild-type enzyme
C1318Y
-
naturally occuring single nucleotide polymorphism, the mutant variant shows reduced activity compared to the wild-type enzyme
D1109T
-
naturally occuring nonsynonymous single nucleotide polymorphism
E308V
-
site-directed mutagenesis, mutant molybdopterin domain structure, overview, the xanthine oxidase changes its substrate specificity to aldehyde oxidase type upon mutation of amino acid residues in the active site, the E803V mutation almost completely abrogates the activity towards hypoxanthine as a substrate, but the decrease in activity towards purine substrate is not due to large conformational change in the mutant enzyme
G172R
-
naturally occuring nonsynonymous single nucleotide polymorphism
H1221R
-
naturally occuring nonsynonymous single nucleotide polymorphism, the mutant variant shows about twofold increased activity compared to the wild-type enzyme
I703V
-
naturally occuring single nucleotide polymorphism, the mutant variant shows abput twofold increased activity compared to the wild-type enzyme
N909K
-
naturally occuring single nucleotide polymorphism, the mutant variant shows reduced activity compared to the wild-type enzyme
P1150R
-
naturally occuring single nucleotide polymorphism, the mutant variant shows reduced activity compared to the wild-type enzyme
P555S
-
naturally occuring single nucleotide polymorphism, the mutant variant shows reduced activity compared to the wild-type enzyme
R149C
-
naturally occuring single nucleotide polymorphism, inactive mutant
R607Q
-
naturally occuring single nucleotide polymorphism, the mutant variant shows reduced activity compared to the wild-type enzyme
R881M
-
site-directed mutagenesis, the xanthine oxidase changes its substrate specificity to aldehyde oxidase type upon mutation of amino acid residues in the active site, the R881M mutant lacks activity towards xanthine, but retaines slight activity towards hypoxanthine
T109K
-
naturally occuring single nucleotide polymorphism, inactive mutant
T623I
-
naturally occuring single nucleotide polymorphism, the mutant variant shows reduced activity compared to the wild-type enzyme
C535A/C992R
site-directed mutagenesis, the mutant activity in the presence of sulfhydryl residue modifiers is very low
C535A/C992R/C1316S
site-directed mutagenesis, the triple mutant does not undergo conversion from XOR, EC 1.17.3.2, to XDH, EC 1.17.1.4, at all
C535A/C992R/C1324S
site-directed mutagenesis, the triple mutant does not undergo conversion from XOR, EC 1.17.3.2, to XDH, EC 1.17.1.4, at all
W335A/F336L
E232A
site-directed mutagenesis, the mutant exhibits a 12fold decrease in kred compared to wild-type
E232Q
site-directed mutagenesis, kred, the limiting rate constant for reduction at high [xanthine], is significantly compromised in the mutant variant E232Q, the mutant exhibits a 12fold decrease in kred, a result that is inconsistent with Glu232 being neutral in the active site of the wild-type enzyme
additional information