Aldehyde oxidase 1; Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Also plays a role in the reductive metabolism of the xenobiotic imid [...]

Aldehyde oxidase 2; Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as phthalazine, as well as aldehydes, such as benzaldehyde and retinal. Cannot use hypoxanthine as substrate.

Aldehyde oxidase 1; Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Also plays a role in the reductive metabolism of the xenobiotic imid [...]

Aldehyde oxidase 3; Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and phthalazine, as well as aldehydes, such as benzaldehyde, retinal and pyridoxal. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the reduction of nitrite to NO with N [...]

Aldehyde oxidase 1; Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Also plays a role in the reductive metabolism of the xenobiotic imid [...]

Aldehyde oxidase 4; Aldehyde oxidase able to catalyze the oxidation of retinaldehyde into retinoate. Is responsible for the major all-trans- retinaldehyde-metabolizing activity in the Harderian gland, and contributes a significant amount of the same activity in the skin. Is devoid of pyridoxal-oxidizing activity, in contrast to the other aldehyde oxidases. Acts as a negative modulator of the epidermal trophism. May be able to oxidize a wide variety of aldehydes into their corresponding carboxylates and to hydroxylate azaheterocycles. Belongs to the xanthine dehydrogenase family.

Aldehyde oxidase 1; Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Also plays a role in the reductive metabolism of the xenobiotic imid [...]

Xanthine dehydrogenase/oxidase; Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species.

Aldehyde oxidase 2; Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as phthalazine, as well as aldehydes, such as benzaldehyde and retinal. Cannot use hypoxanthine as substrate.

Aldehyde oxidase 1; Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Also plays a role in the reductive metabolism of the xenobiotic imid [...]

Aldehyde oxidase 2; Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as phthalazine, as well as aldehydes, such as benzaldehyde and retinal. Cannot use hypoxanthine as substrate.

Aldehyde oxidase 3; Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and phthalazine, as well as aldehydes, such as benzaldehyde, retinal and pyridoxal. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the reduction of nitrite to NO with N [...]

Aldehyde oxidase 2; Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as phthalazine, as well as aldehydes, such as benzaldehyde and retinal. Cannot use hypoxanthine as substrate.

Aldehyde oxidase 4; Aldehyde oxidase able to catalyze the oxidation of retinaldehyde into retinoate. Is responsible for the major all-trans- retinaldehyde-metabolizing activity in the Harderian gland, and contributes a significant amount of the same activity in the skin. Is devoid of pyridoxal-oxidizing activity, in contrast to the other aldehyde oxidases. Acts as a negative modulator of the epidermal trophism. May be able to oxidize a wide variety of aldehydes into their corresponding carboxylates and to hydroxylate azaheterocycles. Belongs to the xanthine dehydrogenase family.

Aldehyde oxidase 2; Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as phthalazine, as well as aldehydes, such as benzaldehyde and retinal. Cannot use hypoxanthine as substrate.

Xanthine dehydrogenase/oxidase; Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species.

Aldehyde oxidase 3; Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and phthalazine, as well as aldehydes, such as benzaldehyde, retinal and pyridoxal. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the reduction of nitrite to NO with N [...]

Aldehyde oxidase 1; Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Also plays a role in the reductive metabolism of the xenobiotic imid [...]

Aldehyde oxidase 3; Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and phthalazine, as well as aldehydes, such as benzaldehyde, retinal and pyridoxal. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the reduction of nitrite to NO with N [...]

Aldehyde oxidase 2; Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as phthalazine, as well as aldehydes, such as benzaldehyde and retinal. Cannot use hypoxanthine as substrate.

Aldehyde oxidase 3; Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and phthalazine, as well as aldehydes, such as benzaldehyde, retinal and pyridoxal. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the reduction of nitrite to NO with N [...]

Aldehyde oxidase 4; Aldehyde oxidase able to catalyze the oxidation of retinaldehyde into retinoate. Is responsible for the major all-trans- retinaldehyde-metabolizing activity in the Harderian gland, and contributes a significant amount of the same activity in the skin. Is devoid of pyridoxal-oxidizing activity, in contrast to the other aldehyde oxidases. Acts as a negative modulator of the epidermal trophism. May be able to oxidize a wide variety of aldehydes into their corresponding carboxylates and to hydroxylate azaheterocycles. Belongs to the xanthine dehydrogenase family.

Aldehyde oxidase 4; Aldehyde oxidase able to catalyze the oxidation of retinaldehyde into retinoate. Is responsible for the major all-trans- retinaldehyde-metabolizing activity in the Harderian gland, and contributes a significant amount of the same activity in the skin. Is devoid of pyridoxal-oxidizing activity, in contrast to the other aldehyde oxidases. Acts as a negative modulator of the epidermal trophism. May be able to oxidize a wide variety of aldehydes into their corresponding carboxylates and to hydroxylate azaheterocycles. Belongs to the xanthine dehydrogenase family.

Aldehyde oxidase 1; Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Also plays a role in the reductive metabolism of the xenobiotic imid [...]

Aldehyde oxidase 4; Aldehyde oxidase able to catalyze the oxidation of retinaldehyde into retinoate. Is responsible for the major all-trans- retinaldehyde-metabolizing activity in the Harderian gland, and contributes a significant amount of the same activity in the skin. Is devoid of pyridoxal-oxidizing activity, in contrast to the other aldehyde oxidases. Acts as a negative modulator of the epidermal trophism. May be able to oxidize a wide variety of aldehydes into their corresponding carboxylates and to hydroxylate azaheterocycles. Belongs to the xanthine dehydrogenase family.

Aldehyde oxidase 2; Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as phthalazine, as well as aldehydes, such as benzaldehyde and retinal. Cannot use hypoxanthine as substrate.

Aldehyde oxidase 4; Aldehyde oxidase able to catalyze the oxidation of retinaldehyde into retinoate. Is responsible for the major all-trans- retinaldehyde-metabolizing activity in the Harderian gland, and contributes a significant amount of the same activity in the skin. Is devoid of pyridoxal-oxidizing activity, in contrast to the other aldehyde oxidases. Acts as a negative modulator of the epidermal trophism. May be able to oxidize a wide variety of aldehydes into their corresponding carboxylates and to hydroxylate azaheterocycles. Belongs to the xanthine dehydrogenase family.

Aldehyde oxidase 3; Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and phthalazine, as well as aldehydes, such as benzaldehyde, retinal and pyridoxal. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the reduction of nitrite to NO with N [...]

Developmentally-regulated GTP-binding protein 1; Catalyzes the conversion of GTP to GDP through hydrolysis of the gamma-phosphate bond in GTP. Appears to have an intrinsic GTPase activity that is stimulated by ZC3H15/DFRP1 binding likely by increasing the affinity for the potassium ions. When hydroxylated at C- 3 of 'Lys-22' by JMJD7, may bind to RNA and play a role in translation. Binds to microtubules and promotes microtubule polymerization and bundling that are required for mitotic spindle assembly during prophase to anaphase transition. GTPase activity is not necessary for these mi [...]

Developmentally-regulated GTP-binding protein 2; Catalyzes the conversion of GTP to GDP through hydrolysis of the gamma-phosphate bond in GTP. When hydroxylated at C-3 of 'Lys-21' by JMJD7, may bind to RNA and play a role in translation. Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family.

Developmentally-regulated GTP-binding protein 2; Catalyzes the conversion of GTP to GDP through hydrolysis of the gamma-phosphate bond in GTP. When hydroxylated at C-3 of 'Lys-21' by JMJD7, may bind to RNA and play a role in translation. Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family.

Developmentally-regulated GTP-binding protein 1; Catalyzes the conversion of GTP to GDP through hydrolysis of the gamma-phosphate bond in GTP. Appears to have an intrinsic GTPase activity that is stimulated by ZC3H15/DFRP1 binding likely by increasing the affinity for the potassium ions. When hydroxylated at C- 3 of 'Lys-22' by JMJD7, may bind to RNA and play a role in translation. Binds to microtubules and promotes microtubule polymerization and bundling that are required for mitotic spindle assembly during prophase to anaphase transition. GTPase activity is not necessary for these mi [...]

Developmentally-regulated GTP-binding protein 2; Catalyzes the conversion of GTP to GDP through hydrolysis of the gamma-phosphate bond in GTP. When hydroxylated at C-3 of 'Lys-21' by JMJD7, may bind to RNA and play a role in translation. Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family.

Threonine--tRNA ligase 1, cytoplasmic; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged tRNA(Thr) via its editing domain, at the post- transfer stage; Belongs to the class-II aminoacyl-tRNA synthetase family.

Developmentally-regulated GTP-binding protein 2; Catalyzes the conversion of GTP to GDP through hydrolysis of the gamma-phosphate bond in GTP. When hydroxylated at C-3 of 'Lys-21' by JMJD7, may bind to RNA and play a role in translation. Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family.

Threonine--tRNA ligase, mitochondrial; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged tRNA(Thr) via its editing domain. Belongs to the class-II aminoacyl-tRNA synthetase family.

Adrenodoxin, mitochondrial; Essential for the synthesis of various steroid hormones, participates in the reduction of mitochondrial cytochrome P450 for steroidogenesis. Transfers electrons from adrenodoxin reductase to CYP11A1, a cytochrome P450 that catalyzes cholesterol side-chain cleavage. Does not form a ternary complex with adrenodoxin reductase and CYP11A1 but shuttles between the two enzymes to transfer electrons. Belongs to the adrenodoxin/putidaredoxin family.

Ferredoxin-2, mitochondrial; Essential for heme A and Fe/S protein biosynthesis. Belongs to the adrenodoxin/putidaredoxin family.

Ferredoxin-2, mitochondrial; Essential for heme A and Fe/S protein biosynthesis. Belongs to the adrenodoxin/putidaredoxin family.

Adrenodoxin, mitochondrial; Essential for the synthesis of various steroid hormones, participates in the reduction of mitochondrial cytochrome P450 for steroidogenesis. Transfers electrons from adrenodoxin reductase to CYP11A1, a cytochrome P450 that catalyzes cholesterol side-chain cleavage. Does not form a ternary complex with adrenodoxin reductase and CYP11A1 but shuttles between the two enzymes to transfer electrons. Belongs to the adrenodoxin/putidaredoxin family.