Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.17.3.2 extracted from

  • Cao, H.; Pauff, J.M.; Hille, R.
    Substrate orientation and catalytic specificity in the action of xanthine oxidase: the sequential hydroxylation of hypoxanthine to uric acid (2010), J. Biol. Chem., 285, 28044-28053.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.17.3.2

Crystallization (Commentary)

Crystallization (Comment) Organism
purified enzyme in complex with hypoxanthine or 6-mercaptopurine, mixing of 0.01 ml of 5 mg/ml protein solution with 0.005-0.006 ml of 12% polyethylene glycol 8000 solution, at pH 7.0, crystallization in the darkness at 25°C, ligand binding by soaking of crystals, X-ray diffraction structure determination and analysis at 1.8 and 2.6 A resolution, respectively Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state and reductive half-reaction rapid kinetics at pH 7.0 and pH 8.5, overview Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Bos taurus
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
xanthine + H2O + O2 Bos taurus
-
 urate + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Bos taurus P80457
-
-

Reaction

Reaction Comment Organism Reaction ID
xanthine + H2O + O2 = urate + H2O2 reaction mechanism for xanthine oxidase, overview. Catalysis is initiated by base-assisted nucleophilic attack of the equatorial Mo-OH on the C-8 carbon of xanthine with concomitant hydride transfer from C-8 to Mo=S, which simultaneously results in reduction of Mo(VI) to Mo(IV). Reoxidation of the molybdenum center occurs by electron transfer to the other redox-active centers of the enzyme, accompanied by deprotonation of the Mo-SH bond and displacement of bound product by hydroxide from solvent to regenerate the Mo-OH group Bos taurus
a

Source Tissue

Source Tissue Comment Organism Textmining
milk
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6,8-dihydroxypurine + H2O + O2 6,8-dihydroxypurine binding structure, overview Bos taurus ? + H2O2
-
 ?
hypoxanthine + 2 H2O + 2 O2 hypoxanthine binding structure, overview Bos taurus urate + 2 H2O2
-
 ?
xanthine + H2O + O2
-
 Bos taurus urate + H2O2
-
 ?
xanthine + H2O + O2 substrate orientation and catalytic specificity, overview Bos taurus urate + H2O2
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Bos taurus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Bos taurus