Literature summary extracted from

Zikakis, J.P.; Dressel, M.A.; Silver, M.R.
Bovine, caprine, and human milk xanthine oxidases: isolation, purification, and characterization (1983), Instrum. Anal. Foods, Recent Prog. (Proc. Symp. Int. Flavor Conf. , 3rd Ed. , Charalambous, G. , Inglett, G. , eds. ), 2, 243-303.

No PubMed abstract available

General Stability

EC Number	General Stability	Organism
1.17.3.2	the enzyme from animal tissues can be interconverted to EC 1.1.1.204, that from liver exists in vivo mainly as the dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Cavia porcellus
1.17.3.2	the enzyme from animal tissues can be interconverted to EC 1.1.1.204, that from liver exists in vivo mainly as the dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Mus musculus
1.17.3.2	the enzyme from animal tissues can be interconverted to EC 1.1.1.204, that from liver exists in vivo mainly as the dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Homo sapiens
1.17.3.2	the enzyme from animal tissues can be interconverted to EC 1.1.1.204, that from liver exists in vivo mainly as the dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Rattus norvegicus
1.17.3.2	the enzyme from animal tissues can be interconverted to EC 1.1.1.204, that from liver exists in vivo mainly as the dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Bos taurus
1.17.3.2	the enzyme from animal tissues can be interconverted to EC 1.1.1.204, that from liver exists in vivo mainly as the dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Oryctolagus cuniculus
1.17.3.2	the enzyme from animal tissues can be interconverted to EC 1.1.1.204, that from liver exists in vivo mainly as the dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Ovis aries
1.17.3.2	the enzyme from animal tissues can be interconverted to EC 1.1.1.204, that from liver exists in vivo mainly as the dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Canis lupus familiaris
1.17.3.2	the enzyme from animal tissues can be interconverted to EC 1.1.1.204, that from liver exists in vivo mainly as the dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Felis catus
1.17.3.2	the enzyme from animal tissues can be interconverted to EC 1.1.1.204, that from liver exists in vivo mainly as the dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Capra hircus
1.17.3.2	the enzyme from animal tissues can be interconverted to EC 1.1.1.204, that from liver exists in vivo mainly as the dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Equus caballus
1.17.3.2	the enzyme from animal tissues can be interconverted to EC 1.1.1.204, that from liver exists in vivo mainly as the dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Equus asinus
1.17.3.2	the enzyme from animal tissues can be interconverted to EC 1.1.1.204, that from liver exists in vivo mainly as the dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Erythrocebus patas

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
1.17.3.2	additional information	-	additional information	-	Cavia porcellus
1.17.3.2	additional information	-	additional information	-	Mus musculus
1.17.3.2	additional information	-	additional information	-	Homo sapiens
1.17.3.2	additional information	-	additional information	-	Rattus norvegicus
1.17.3.2	additional information	-	additional information	-	Bos taurus
1.17.3.2	additional information	-	additional information	-	Oryctolagus cuniculus
1.17.3.2	additional information	-	additional information	-	Ovis aries
1.17.3.2	additional information	-	additional information	-	Canis lupus familiaris
1.17.3.2	additional information	-	additional information	-	Felis catus
1.17.3.2	additional information	-	additional information	-	Capra hircus
1.17.3.2	additional information	-	additional information	-	Equus caballus
1.17.3.2	additional information	-	additional information	-	Equus asinus
1.17.3.2	additional information	-	additional information	-	Erythrocebus patas
1.17.3.2	0.00924	-	hypoxanthine	membrane-bound enzyme	Homo sapiens
1.17.3.2	0.0134	-	hypoxanthine	free enzyme	Homo sapiens
1.17.3.2	0.0264	-	xanthine	membrane-bound enzyme	Homo sapiens
1.17.3.2	0.0279	-	xanthine	free enzyme	Homo sapiens

Localization

EC Number	Localization	Comment	Organism	GeneOntology No.	Textmining
1.17.3.2	lipid droplet	-	Bos taurus	5811	-
1.17.3.2	lipid droplet	membrane-bound	Felis catus	5811	-

Metals/Ions

EC Number	Metals/Ions	Comment	Organism
1.17.3.2	Iron	iron-molybdenum protein	Cavia porcellus
1.17.3.2	Iron	iron-molybdenum protein	Mus musculus
1.17.3.2	Iron	iron-molybdenum protein	Homo sapiens
1.17.3.2	Iron	iron-molybdenum protein	Rattus norvegicus
1.17.3.2	Iron	iron-molybdenum protein	Bos taurus
1.17.3.2	Iron	iron-molybdenum protein	Oryctolagus cuniculus
1.17.3.2	Iron	iron-molybdenum protein	Ovis aries
1.17.3.2	Iron	iron-molybdenum protein	Canis lupus familiaris
1.17.3.2	Iron	iron-molybdenum protein	Felis catus
1.17.3.2	Iron	iron-molybdenum protein	Capra hircus
1.17.3.2	Iron	iron-molybdenum protein	Equus caballus
1.17.3.2	Iron	iron-molybdenum protein	Equus asinus
1.17.3.2	Iron	iron-molybdenum protein	Erythrocebus patas
1.17.3.2	Molybdenum	an iron-molybdenum protein	Cavia porcellus
1.17.3.2	Molybdenum	an iron-molybdenum protein	Mus musculus
1.17.3.2	Molybdenum	an iron-molybdenum protein	Homo sapiens
1.17.3.2	Molybdenum	an iron-molybdenum protein	Rattus norvegicus
1.17.3.2	Molybdenum	an iron-molybdenum protein	Bos taurus
1.17.3.2	Molybdenum	an iron-molybdenum protein	Oryctolagus cuniculus
1.17.3.2	Molybdenum	an iron-molybdenum protein	Ovis aries
1.17.3.2	Molybdenum	an iron-molybdenum protein	Canis lupus familiaris
1.17.3.2	Molybdenum	an iron-molybdenum protein	Felis catus
1.17.3.2	Molybdenum	an iron-molybdenum protein	Capra hircus
1.17.3.2	Molybdenum	an iron-molybdenum protein	Equus caballus
1.17.3.2	Molybdenum	an iron-molybdenum protein	Equus asinus
1.17.3.2	Molybdenum	an iron-molybdenum protein	Erythrocebus patas

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
1.17.3.2	310000	-	gel filtration	Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
1.17.3.2	carboxylic aldehyde + H2O + O2	Cavia porcellus	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	Mus musculus	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	Homo sapiens	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	Rattus norvegicus	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	Bos taurus	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	Oryctolagus cuniculus	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	Ovis aries	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	Canis lupus familiaris	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	Felis catus	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	Capra hircus	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	Equus caballus	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	Equus asinus	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	Erythrocebus patas	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	Erythrocebus patas Patas monkey	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	carboxylic acid + H2O2	-	?
1.17.3.2	pteridine + H2O + O2	Cavia porcellus	-	?	-	?
1.17.3.2	pteridine + H2O + O2	Mus musculus	-	?	-	?
1.17.3.2	pteridine + H2O + O2	Homo sapiens	-	?	-	?
1.17.3.2	pteridine + H2O + O2	Rattus norvegicus	-	?	-	?
1.17.3.2	pteridine + H2O + O2	Bos taurus	-	?	-	?
1.17.3.2	pteridine + H2O + O2	Oryctolagus cuniculus	-	?	-	?
1.17.3.2	pteridine + H2O + O2	Ovis aries	-	?	-	?
1.17.3.2	pteridine + H2O + O2	Canis lupus familiaris	-	?	-	?
1.17.3.2	pteridine + H2O + O2	Felis catus	-	?	-	?
1.17.3.2	pteridine + H2O + O2	Capra hircus	-	?	-	?
1.17.3.2	pteridine + H2O + O2	Equus caballus	-	?	-	?
1.17.3.2	pteridine + H2O + O2	Equus asinus	-	?	-	?
1.17.3.2	pteridine + H2O + O2	Erythrocebus patas	-	?	-	?
1.17.3.2	pteridine + H2O + O2	Erythrocebus patas Patas monkey	-	?	-	?
1.17.3.2	purine + H2O + O2	Cavia porcellus	-	?	-	?
1.17.3.2	purine + H2O + O2	Mus musculus	-	?	-	?
1.17.3.2	purine + H2O + O2	Homo sapiens	-	?	-	?
1.17.3.2	purine + H2O + O2	Rattus norvegicus	-	?	-	?
1.17.3.2	purine + H2O + O2	Bos taurus	-	?	-	?
1.17.3.2	purine + H2O + O2	Oryctolagus cuniculus	-	?	-	?
1.17.3.2	purine + H2O + O2	Ovis aries	-	?	-	?
1.17.3.2	purine + H2O + O2	Canis lupus familiaris	-	?	-	?
1.17.3.2	purine + H2O + O2	Felis catus	-	?	-	?
1.17.3.2	purine + H2O + O2	Capra hircus	-	?	-	?
1.17.3.2	purine + H2O + O2	Equus caballus	-	?	-	?
1.17.3.2	purine + H2O + O2	Equus asinus	-	?	-	?
1.17.3.2	purine + H2O + O2	Erythrocebus patas	-	?	-	?
1.17.3.2	purine + H2O + O2	Erythrocebus patas Patas monkey	-	?	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.17.3.2	Bos taurus	-	-	-
1.17.3.2	Canis lupus familiaris	-	-	-
1.17.3.2	Capra hircus	-	-	-
1.17.3.2	Cavia porcellus	-	-	-
1.17.3.2	Equus asinus	-	-	-
1.17.3.2	Equus caballus	-	-	-
1.17.3.2	Erythrocebus patas	-	Patas monkey	-
1.17.3.2	Erythrocebus patas Patas monkey	-	Patas monkey	-
1.17.3.2	Felis catus	-	-	-
1.17.3.2	Homo sapiens	-	-	-
1.17.3.2	Mus musculus	-	-	-
1.17.3.2	Oryctolagus cuniculus	-	-	-
1.17.3.2	Ovis aries	-	-	-
1.17.3.2	Rattus norvegicus	-	-	-

Posttranslational Modification

EC Number	Posttranslational Modification	Comment	Organism
1.17.3.2	additional information	the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Cavia porcellus
1.17.3.2	additional information	the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Mus musculus
1.17.3.2	additional information	the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Homo sapiens
1.17.3.2	additional information	the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Rattus norvegicus
1.17.3.2	additional information	the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Bos taurus
1.17.3.2	additional information	the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Oryctolagus cuniculus
1.17.3.2	additional information	the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Ovis aries
1.17.3.2	additional information	the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Canis lupus familiaris
1.17.3.2	additional information	the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Felis catus
1.17.3.2	additional information	the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Capra hircus
1.17.3.2	additional information	the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Equus caballus
1.17.3.2	additional information	the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Equus asinus
1.17.3.2	additional information	the enzyme from animal tissues can be interconverted to xanthine dehydrogenase, EC 1.1.1.204, the liver enzyme exists in vivo mainly in its dehydrogenase form, but can be converted into the oxidase form by storage at -20°C, by treatment with proteolytic enzymes or with organic solvents, or by thiol reagents such as Cu2+, N-ethylmaleimide or 4-hydroxymercuribenzoate, the effect of the thiol reagents can be reversed by thiols such as 1,4-dithioerythritol, in other animal tissues the enzyme exists almost entirely as EC 1.1.3.22 but can be converted into the dehydrogenase form by 1,4-dithioerythritol	Erythrocebus patas
1.17.3.2	proteolytic modification	-	Cavia porcellus
1.17.3.2	proteolytic modification	-	Mus musculus
1.17.3.2	proteolytic modification	-	Homo sapiens
1.17.3.2	proteolytic modification	-	Rattus norvegicus
1.17.3.2	proteolytic modification	-	Bos taurus
1.17.3.2	proteolytic modification	-	Oryctolagus cuniculus
1.17.3.2	proteolytic modification	-	Ovis aries
1.17.3.2	proteolytic modification	-	Canis lupus familiaris
1.17.3.2	proteolytic modification	-	Felis catus
1.17.3.2	proteolytic modification	-	Capra hircus
1.17.3.2	proteolytic modification	-	Equus caballus
1.17.3.2	proteolytic modification	-	Equus asinus
1.17.3.2	proteolytic modification	-	Erythrocebus patas

Purification (Commentary)

EC Number	Purification (Comment)	Organism
1.17.3.2	-	Homo sapiens
1.17.3.2	-	Bos taurus
1.17.3.2	-	Capra hircus

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
1.17.3.2	colostrum	-	Cavia porcellus	-
1.17.3.2	colostrum	-	Mus musculus	-
1.17.3.2	colostrum	-	Homo sapiens	-
1.17.3.2	colostrum	-	Rattus norvegicus	-
1.17.3.2	colostrum	-	Bos taurus	-
1.17.3.2	colostrum	-	Oryctolagus cuniculus	-
1.17.3.2	colostrum	-	Ovis aries	-
1.17.3.2	colostrum	-	Canis lupus familiaris	-
1.17.3.2	colostrum	-	Felis catus	-
1.17.3.2	colostrum	-	Capra hircus	-
1.17.3.2	colostrum	-	Equus caballus	-
1.17.3.2	colostrum	-	Equus asinus	-
1.17.3.2	colostrum	-	Erythrocebus patas	-
1.17.3.2	liver	-	Cavia porcellus	-
1.17.3.2	liver	-	Mus musculus	-
1.17.3.2	liver	-	Homo sapiens	-
1.17.3.2	liver	-	Rattus norvegicus	-
1.17.3.2	liver	-	Bos taurus	-
1.17.3.2	liver	-	Oryctolagus cuniculus	-
1.17.3.2	liver	-	Ovis aries	-
1.17.3.2	liver	-	Canis lupus familiaris	-
1.17.3.2	liver	-	Felis catus	-
1.17.3.2	liver	-	Capra hircus	-
1.17.3.2	liver	-	Equus caballus	-
1.17.3.2	liver	-	Equus asinus	-
1.17.3.2	liver	-	Erythrocebus patas	-
1.17.3.2	milk	-	Cavia porcellus	-
1.17.3.2	milk	-	Mus musculus	-
1.17.3.2	milk	-	Homo sapiens	-
1.17.3.2	milk	-	Rattus norvegicus	-
1.17.3.2	milk	-	Bos taurus	-
1.17.3.2	milk	-	Oryctolagus cuniculus	-
1.17.3.2	milk	-	Ovis aries	-
1.17.3.2	milk	-	Canis lupus familiaris	-
1.17.3.2	milk	-	Felis catus	-
1.17.3.2	milk	-	Capra hircus	-
1.17.3.2	milk	-	Equus caballus	-
1.17.3.2	milk	-	Equus asinus	-
1.17.3.2	milk	-	Erythrocebus patas	-

Specific Activity [micromol/min/mg]

EC Number	Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
1.17.3.2	2.04	-	colostrum	Homo sapiens
1.17.3.2	7.8	-	milk	Bos taurus
1.17.3.2	123	-	milk	Capra hircus

Storage Stability

EC Number	Storage Stability	Organism
1.17.3.2	-20°C, 27% loss of activity after 2 weeks, 51% loss of activity after 4 weeks, 89% loss of activity after 12 weeks, goat enzyme	Capra hircus
1.17.3.2	4°C, 31% loss of activity after 6 days, 54% loss of activity after 12 days, 72% loss of activity after 16 days, goat enzyme	Capra hircus

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
1.17.3.2	carboxylic aldehyde + H2O + O2	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	Cavia porcellus	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	Mus musculus	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	Homo sapiens	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	Rattus norvegicus	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	Bos taurus	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	Oryctolagus cuniculus	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	Ovis aries	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	Canis lupus familiaris	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	Felis catus	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	Capra hircus	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	Equus caballus	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	Equus asinus	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	Erythrocebus patas	carboxylic acid + H2O2	-	?
1.17.3.2	carboxylic aldehyde + H2O + O2	enzyme is implicated in the control of various redox reactions in the cell, in milk: assures absorption of iron from the gut, coupling antibacterial effect via the lactoperoxidase system	Erythrocebus patas Patas monkey	carboxylic acid + H2O2	-	?
1.17.3.2	hypoxanthine + 2 H2O + 2 O2	-	Cavia porcellus	urate + 2 H2O2	-	?
1.17.3.2	hypoxanthine + 2 H2O + 2 O2	-	Mus musculus	urate + 2 H2O2	-	?
1.17.3.2	hypoxanthine + 2 H2O + 2 O2	-	Homo sapiens	urate + 2 H2O2	-	?
1.17.3.2	hypoxanthine + 2 H2O + 2 O2	-	Rattus norvegicus	urate + 2 H2O2	-	?
1.17.3.2	hypoxanthine + 2 H2O + 2 O2	-	Bos taurus	urate + 2 H2O2	-	?
1.17.3.2	hypoxanthine + 2 H2O + 2 O2	-	Oryctolagus cuniculus	urate + 2 H2O2	-	?
1.17.3.2	hypoxanthine + 2 H2O + 2 O2	-	Ovis aries	urate + 2 H2O2	-	?
1.17.3.2	hypoxanthine + 2 H2O + 2 O2	-	Canis lupus familiaris	urate + 2 H2O2	-	?
1.17.3.2	hypoxanthine + 2 H2O + 2 O2	-	Felis catus	urate + 2 H2O2	-	?
1.17.3.2	hypoxanthine + 2 H2O + 2 O2	-	Capra hircus	urate + 2 H2O2	-	?
1.17.3.2	hypoxanthine + 2 H2O + 2 O2	-	Equus caballus	urate + 2 H2O2	-	?
1.17.3.2	hypoxanthine + 2 H2O + 2 O2	-	Equus asinus	urate + 2 H2O2	-	?
1.17.3.2	hypoxanthine + 2 H2O + 2 O2	-	Erythrocebus patas	urate + 2 H2O2	-	?
1.17.3.2	hypoxanthine + 2 H2O + 2 O2	-	Erythrocebus patas Patas monkey	urate + 2 H2O2	-	?
1.17.3.2	pteridine + H2O + O2	-	Cavia porcellus	?	-	?
1.17.3.2	pteridine + H2O + O2	-	Mus musculus	?	-	?
1.17.3.2	pteridine + H2O + O2	-	Homo sapiens	?	-	?
1.17.3.2	pteridine + H2O + O2	-	Rattus norvegicus	?	-	?
1.17.3.2	pteridine + H2O + O2	-	Bos taurus	?	-	?
1.17.3.2	pteridine + H2O + O2	-	Oryctolagus cuniculus	?	-	?
1.17.3.2	pteridine + H2O + O2	-	Ovis aries	?	-	?
1.17.3.2	pteridine + H2O + O2	-	Canis lupus familiaris	?	-	?
1.17.3.2	pteridine + H2O + O2	-	Felis catus	?	-	?
1.17.3.2	pteridine + H2O + O2	-	Capra hircus	?	-	?
1.17.3.2	pteridine + H2O + O2	-	Equus caballus	?	-	?
1.17.3.2	pteridine + H2O + O2	-	Equus asinus	?	-	?
1.17.3.2	pteridine + H2O + O2	-	Erythrocebus patas	?	-	?
1.17.3.2	pteridine + H2O + O2	-	Erythrocebus patas Patas monkey	?	-	?
1.17.3.2	purine + H2O + O2	-	Cavia porcellus	?	-	?
1.17.3.2	purine + H2O + O2	-	Mus musculus	?	-	?
1.17.3.2	purine + H2O + O2	-	Homo sapiens	?	-	?
1.17.3.2	purine + H2O + O2	-	Rattus norvegicus	?	-	?
1.17.3.2	purine + H2O + O2	-	Bos taurus	?	-	?
1.17.3.2	purine + H2O + O2	-	Oryctolagus cuniculus	?	-	?
1.17.3.2	purine + H2O + O2	-	Ovis aries	?	-	?
1.17.3.2	purine + H2O + O2	-	Canis lupus familiaris	?	-	?
1.17.3.2	purine + H2O + O2	-	Felis catus	?	-	?
1.17.3.2	purine + H2O + O2	-	Capra hircus	?	-	?
1.17.3.2	purine + H2O + O2	-	Equus caballus	?	-	?
1.17.3.2	purine + H2O + O2	-	Equus asinus	?	-	?
1.17.3.2	purine + H2O + O2	-	Erythrocebus patas	?	-	?
1.17.3.2	purine + H2O + O2	-	Erythrocebus patas Patas monkey	?	-	?
1.17.3.2	xanthine + H2O + O2	electron acceptor O2	Cavia porcellus	uric acid + H2O2	-	?
1.17.3.2	xanthine + H2O + O2	electron acceptor O2	Mus musculus	uric acid + H2O2	-	?
1.17.3.2	xanthine + H2O + O2	electron acceptor O2	Homo sapiens	uric acid + H2O2	-	?
1.17.3.2	xanthine + H2O + O2	electron acceptor O2	Rattus norvegicus	uric acid + H2O2	-	?
1.17.3.2	xanthine + H2O + O2	electron acceptor O2	Bos taurus	uric acid + H2O2	-	?
1.17.3.2	xanthine + H2O + O2	electron acceptor O2	Oryctolagus cuniculus	uric acid + H2O2	-	?
1.17.3.2	xanthine + H2O + O2	electron acceptor O2	Ovis aries	uric acid + H2O2	-	?
1.17.3.2	xanthine + H2O + O2	electron acceptor O2	Canis lupus familiaris	uric acid + H2O2	-	?
1.17.3.2	xanthine + H2O + O2	electron acceptor O2	Felis catus	uric acid + H2O2	-	?
1.17.3.2	xanthine + H2O + O2	electron acceptor O2	Capra hircus	uric acid + H2O2	-	?
1.17.3.2	xanthine + H2O + O2	electron acceptor O2	Equus caballus	uric acid + H2O2	-	?
1.17.3.2	xanthine + H2O + O2	electron acceptor O2	Equus asinus	uric acid + H2O2	-	?
1.17.3.2	xanthine + H2O + O2	electron acceptor O2	Erythrocebus patas	uric acid + H2O2	-	?
1.17.3.2	xanthine + H2O + O2	electron acceptor O2	Erythrocebus patas Patas monkey	uric acid + H2O2	-	?

Temperature Optimum [°C]

EC Number	Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
1.17.3.2	23	-	assay at	Cavia porcellus
1.17.3.2	23	-	assay at	Mus musculus
1.17.3.2	23	-	assay at	Homo sapiens
1.17.3.2	23	-	assay at	Rattus norvegicus
1.17.3.2	23	-	assay at	Bos taurus
1.17.3.2	23	-	assay at	Oryctolagus cuniculus
1.17.3.2	23	-	assay at	Ovis aries
1.17.3.2	23	-	assay at	Canis lupus familiaris
1.17.3.2	23	-	assay at	Felis catus
1.17.3.2	23	-	assay at	Capra hircus
1.17.3.2	23	-	assay at	Equus caballus
1.17.3.2	23	-	assay at	Equus asinus
1.17.3.2	23	-	assay at	Erythrocebus patas

pH Optimum

EC Number	pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
1.17.3.2	8.2	-	-	Homo sapiens
1.17.3.2	8.35	-	-	Capra hircus

Cofactor

EC Number	Cofactor	Comment	Organism
1.17.3.2	FAD	flavoprotein	Cavia porcellus
1.17.3.2	FAD	flavoprotein	Mus musculus
1.17.3.2	FAD	flavoprotein	Homo sapiens
1.17.3.2	FAD	flavoprotein	Rattus norvegicus
1.17.3.2	FAD	flavoprotein	Bos taurus
1.17.3.2	FAD	flavoprotein	Oryctolagus cuniculus
1.17.3.2	FAD	flavoprotein	Ovis aries
1.17.3.2	FAD	flavoprotein	Canis lupus familiaris
1.17.3.2	FAD	flavoprotein	Felis catus
1.17.3.2	FAD	flavoprotein	Capra hircus
1.17.3.2	FAD	flavoprotein	Equus caballus
1.17.3.2	FAD	flavoprotein	Equus asinus
1.17.3.2	FAD	flavoprotein	Erythrocebus patas