Literature summary for 1.17.3.2 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

General Stability	Organism
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
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
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
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
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
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
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
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
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
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
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
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
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]

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

Localization

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

Metals/Ions

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
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	-	?
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	-	?
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	-	?
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	-	?
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	-	?
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	-	?
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	-	?
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	-	?
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	-	?
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	-	?
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	-	?
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	-	?
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	-	?
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	-	?
pteridine + H2O + O2	Cavia porcellus	-	?	-	?
pteridine + H2O + O2	Mus musculus	-	?	-	?
pteridine + H2O + O2	Homo sapiens	-	?	-	?
pteridine + H2O + O2	Rattus norvegicus	-	?	-	?
pteridine + H2O + O2	Bos taurus	-	?	-	?
pteridine + H2O + O2	Oryctolagus cuniculus	-	?	-	?
pteridine + H2O + O2	Ovis aries	-	?	-	?
pteridine + H2O + O2	Canis lupus familiaris	-	?	-	?
pteridine + H2O + O2	Felis catus	-	?	-	?
pteridine + H2O + O2	Capra hircus	-	?	-	?
pteridine + H2O + O2	Equus caballus	-	?	-	?
pteridine + H2O + O2	Equus asinus	-	?	-	?
pteridine + H2O + O2	Erythrocebus patas	-	?	-	?
pteridine + H2O + O2	Erythrocebus patas Patas monkey	-	?	-	?
purine + H2O + O2	Cavia porcellus	-	?	-	?
purine + H2O + O2	Mus musculus	-	?	-	?
purine + H2O + O2	Homo sapiens	-	?	-	?
purine + H2O + O2	Rattus norvegicus	-	?	-	?
purine + H2O + O2	Bos taurus	-	?	-	?
purine + H2O + O2	Oryctolagus cuniculus	-	?	-	?
purine + H2O + O2	Ovis aries	-	?	-	?
purine + H2O + O2	Canis lupus familiaris	-	?	-	?
purine + H2O + O2	Felis catus	-	?	-	?
purine + H2O + O2	Capra hircus	-	?	-	?
purine + H2O + O2	Equus caballus	-	?	-	?
purine + H2O + O2	Equus asinus	-	?	-	?
purine + H2O + O2	Erythrocebus patas	-	?	-	?
purine + H2O + O2	Erythrocebus patas Patas monkey	-	?	-	?

Organism

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

Posttranslational Modification

Posttranslational Modification	Comment	Organism
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
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
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
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
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
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
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
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
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
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
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
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
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
proteolytic modification	-	Cavia porcellus
proteolytic modification	-	Mus musculus
proteolytic modification	-	Homo sapiens
proteolytic modification	-	Rattus norvegicus
proteolytic modification	-	Bos taurus
proteolytic modification	-	Oryctolagus cuniculus
proteolytic modification	-	Ovis aries
proteolytic modification	-	Canis lupus familiaris
proteolytic modification	-	Felis catus
proteolytic modification	-	Capra hircus
proteolytic modification	-	Equus caballus
proteolytic modification	-	Equus asinus
proteolytic modification	-	Erythrocebus patas

Purification (Commentary)

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

Source Tissue

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

Specific Activity [micromol/min/mg]

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

Storage Stability

Storage Stability	Organism
-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
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)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
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	-	?
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	-	?
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	-	?
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	-	?
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	-	?
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	-	?
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	-	?
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	-	?
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	-	?
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	-	?
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	-	?
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	-	?
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	-	?
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	-	?
hypoxanthine + 2 H2O + 2 O2	-	Cavia porcellus	urate + 2 H2O2	-	?
hypoxanthine + 2 H2O + 2 O2	-	Mus musculus	urate + 2 H2O2	-	?
hypoxanthine + 2 H2O + 2 O2	-	Homo sapiens	urate + 2 H2O2	-	?
hypoxanthine + 2 H2O + 2 O2	-	Rattus norvegicus	urate + 2 H2O2	-	?
hypoxanthine + 2 H2O + 2 O2	-	Bos taurus	urate + 2 H2O2	-	?
hypoxanthine + 2 H2O + 2 O2	-	Oryctolagus cuniculus	urate + 2 H2O2	-	?
hypoxanthine + 2 H2O + 2 O2	-	Ovis aries	urate + 2 H2O2	-	?
hypoxanthine + 2 H2O + 2 O2	-	Canis lupus familiaris	urate + 2 H2O2	-	?
hypoxanthine + 2 H2O + 2 O2	-	Felis catus	urate + 2 H2O2	-	?
hypoxanthine + 2 H2O + 2 O2	-	Capra hircus	urate + 2 H2O2	-	?
hypoxanthine + 2 H2O + 2 O2	-	Equus caballus	urate + 2 H2O2	-	?
hypoxanthine + 2 H2O + 2 O2	-	Equus asinus	urate + 2 H2O2	-	?
hypoxanthine + 2 H2O + 2 O2	-	Erythrocebus patas	urate + 2 H2O2	-	?
hypoxanthine + 2 H2O + 2 O2	-	Erythrocebus patas Patas monkey	urate + 2 H2O2	-	?
pteridine + H2O + O2	-	Cavia porcellus	?	-	?
pteridine + H2O + O2	-	Mus musculus	?	-	?
pteridine + H2O + O2	-	Homo sapiens	?	-	?
pteridine + H2O + O2	-	Rattus norvegicus	?	-	?
pteridine + H2O + O2	-	Bos taurus	?	-	?
pteridine + H2O + O2	-	Oryctolagus cuniculus	?	-	?
pteridine + H2O + O2	-	Ovis aries	?	-	?
pteridine + H2O + O2	-	Canis lupus familiaris	?	-	?
pteridine + H2O + O2	-	Felis catus	?	-	?
pteridine + H2O + O2	-	Capra hircus	?	-	?
pteridine + H2O + O2	-	Equus caballus	?	-	?
pteridine + H2O + O2	-	Equus asinus	?	-	?
pteridine + H2O + O2	-	Erythrocebus patas	?	-	?
pteridine + H2O + O2	-	Erythrocebus patas Patas monkey	?	-	?
purine + H2O + O2	-	Cavia porcellus	?	-	?
purine + H2O + O2	-	Mus musculus	?	-	?
purine + H2O + O2	-	Homo sapiens	?	-	?
purine + H2O + O2	-	Rattus norvegicus	?	-	?
purine + H2O + O2	-	Bos taurus	?	-	?
purine + H2O + O2	-	Oryctolagus cuniculus	?	-	?
purine + H2O + O2	-	Ovis aries	?	-	?
purine + H2O + O2	-	Canis lupus familiaris	?	-	?
purine + H2O + O2	-	Felis catus	?	-	?
purine + H2O + O2	-	Capra hircus	?	-	?
purine + H2O + O2	-	Equus caballus	?	-	?
purine + H2O + O2	-	Equus asinus	?	-	?
purine + H2O + O2	-	Erythrocebus patas	?	-	?
purine + H2O + O2	-	Erythrocebus patas Patas monkey	?	-	?
xanthine + H2O + O2	electron acceptor O2	Cavia porcellus	uric acid + H2O2	-	?
xanthine + H2O + O2	electron acceptor O2	Mus musculus	uric acid + H2O2	-	?
xanthine + H2O + O2	electron acceptor O2	Homo sapiens	uric acid + H2O2	-	?
xanthine + H2O + O2	electron acceptor O2	Rattus norvegicus	uric acid + H2O2	-	?
xanthine + H2O + O2	electron acceptor O2	Bos taurus	uric acid + H2O2	-	?
xanthine + H2O + O2	electron acceptor O2	Oryctolagus cuniculus	uric acid + H2O2	-	?
xanthine + H2O + O2	electron acceptor O2	Ovis aries	uric acid + H2O2	-	?
xanthine + H2O + O2	electron acceptor O2	Canis lupus familiaris	uric acid + H2O2	-	?
xanthine + H2O + O2	electron acceptor O2	Felis catus	uric acid + H2O2	-	?
xanthine + H2O + O2	electron acceptor O2	Capra hircus	uric acid + H2O2	-	?
xanthine + H2O + O2	electron acceptor O2	Equus caballus	uric acid + H2O2	-	?
xanthine + H2O + O2	electron acceptor O2	Equus asinus	uric acid + H2O2	-	?
xanthine + H2O + O2	electron acceptor O2	Erythrocebus patas	uric acid + H2O2	-	?
xanthine + H2O + O2	electron acceptor O2	Erythrocebus patas Patas monkey	uric acid + H2O2	-	?

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

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