| Identification | Back Directory | [Name]
EC 1.1.3.22 | [CAS]
9002-17-9 | [Synonyms]
XOD
C:C&B41
e.c.1.2.3.2
EC 1.1.3.22
xanthine-oxidas
XANTHINE OXIDASE
XOD,exbuttermilk
Xanthione oxidase
schardingerenzyme
Oxidase, xanthine
hypoxanthineoxidase
xanthopterin-oxidase
EC 1.1.3.22 USP/EP/BP
xanthineoxidoreductase
xanthine oxidase(cream)
XANTHINE OXIDASE ex butter
XanthineOxidaseExButtermilk
XANTHINE OXIDASE, BUTTERMILK
XANTHINE OXIDASE (MICROBIAL)
XANTHINE OXIDASE, BOVINE MILK
Hypoxanthine-xanthine oxidase
xanthineoxidaseandhypoxanthine
hypoxanthineandxanthineoxidase
XANTHINE:OXYGEN OXIDOREDUCTASE
Native Bovine Xanthine Oxidase
xanthine oxidase from buttermilk
Xanthine Oxidase from bovine milk
Native Microbial Xanthine Oxidase
xanthine oxidase, buttermilk (XOD)
XANTHINE OXIDASE GRADE IV FROM MILK
xanthine oxidase from microorganism
XANTHINE OXIDASE MICROBIAL, >7 U/MG
XOD, Xanthine: oxygen oxidoreductase
Xanthine:oxygen oxidoreductase, XOD
Xanthine Oxidase from Arthrobacter sp.
Xanthine Oxidase, Microbial, 40 units/Mg
xanthine oxidase grade I from*buttermilk
Xanthine Oxidase ex. Microorganism, 15U/mg
XANTHINE OXIDASE GRADE III FROM*BUTTERMI LK
XANTHIN-OXIDASE from buttermilk, ~0.07 U/mg
Xanthine Oxidase [microbial, 5 units/mg solid]
Xanthine Oxidase>95%,>50u/mg Arthrobacter sp.
Xanthine oxidase from buttermilk ca. 1 U/mg protein
XANTHINE OXIDASE FROM BUTTERMILK, LYOPH. ~0.4 U/MG*
Xanthine Oxidase microbial [lyophilized, ≥40 units/mg]
XANTHINE OXIDASE FROM BUTTERMILK SUSP. 1 .25 U/MG PROTEIN
Xanthine Oxidase Suspension ex. Butter Milk, 1-4 U/mg protein
XANTHINE OXIDASE FROM BUTTER-MILK CA.1 U/MG PROTEIN SUSPENSION
Xanthine Oxidase microbial,XOD, Xanthine:oxygen oxidoreductase
tert-butyl 9-oxohexahydro-1H-pyrido[1,2-a]pyrazine-2(6H)-carboxylate
Xanthine Oxidase from bovine milk,XOD, Xanthine:oxygen oxidoreductase | [EINECS(EC#)]
232-657-6 | [Molecular Formula]
N/A | [MDL Number]
MFCD00082145 |
| Hazard Information | Back Directory | [Description]
An enzyme that is closely
related to aldehyde oxidase (EC 1.2.3.1). Both are metalloflavoproteins of about 300,000 daltons. They consist of two subunits of equal size and contain molybdenum, FAD, and iron
(as Fe/S) in a ratio of 1:1:4 per subunit. These enzymes are
widely distributed and catalyze a reaction in which the substrate is hydroxylated by an oxygen atom derived from water
and electrons from the substrate are transferred to a variety of
acceptors. These two enzymes have a broad overlapping substrate specificity including many purines, pyrimidines, and
pteridines. However, xanthine, the best known substrate for
xanthine oxidase, is not a substrate for aldehyde oxidase
whereas the reverse is true for quaternary pyridinium compounds, such as N0
-methylnicotinamide. The role of oxygen as
an electron acceptor with its production of hydrogen peroxide
and the intermediate superoxide anion (both potential toxicants) may not be important in vivo since there is evidence
that these enzymes are NAD-dependent dehydrogenases
in vivo and become oxidases as a result of modification during
purification. However, they are probably important in two
types of detoxication. The first of these is the hydroxylation of
exogenous aldehydes, purines, pyrimidines and other heterocyclic compounds, and the second involves the utilization of
exogenous compounds as electron acceptors. Examples of the
latter include the conversion of organic nitro compounds to
hydroxyamino derivatives and the reduction of N-oxides to the
free base. | [Chemical Properties]
Light brown powder | [Uses]
Biochemical research | [Definition]
An enzyme found in animal
tissues that acts upon hypoxanthine, xanthine, aldehydes,
reduced coenzyme I, etc., producing, respectively,
xanthine, uric acid, acids, oxidized coenzyme
I, etc. | [General Description]
Formerly E.C. 1.1.3.22 | [Biochem/physiol Actions]
Hydroxylation of hypoxanthine to xanthine and xanthine to uric acid is catalyzed by xanthinebb oxidase (XO) enzyme. |
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