Pyridoxal phosphate phosphatase; Protein serine phosphatase that dephosphorylates 'Ser-3' in cofilin and probably also dephosphorylates phospho-serine residues in DSTN. Regulates cofilin-dependent actin cytoskeleton reorganization. Required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phospho-threonines in LIMK1. Does not dephosphorylate peptides containing phospho-tyrosine (By similarity). Pyridoxal phosphate (PLP) phosphatase, which also catalyzes the dephosphorylation of pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'- phosphate (PMP), with [...]

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 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.

Pyridoxal phosphate phosphatase PHOSPHO2; Phosphatase that has high activity toward pyridoxal 5'- phosphate (PLP). Also active at much lower level toward pyrophosphate, phosphoethanolamine (PEA), phosphocholine (PCho), phospho-l-tyrosine, fructose-6-phosphate, p-nitrophenyl phosphate, and h-glycerophosphate (By similarity).

Pyridoxal phosphate homeostasis protein; Pyridoxal 5'-phosphate (PLP)-binding protein, which may be involved in intracellular homeostatic regulation of pyridoxal 5'- phosphate (PLP), the active form of vitamin B6.

Proliferating cell nuclear antigen; Auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'- phosphodiesterase, but not apurinic-apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA rep [...]

Ribosomal RNA processing protein 1 homolog B; Positively regulates DNA damage-induced apoptosis by acting as a transcriptional coactivator of proapoptotic target genes of the transcriptional activator E2F1 (By similarity). Likely to play a role in ribosome biogenesis by targeting serine/threonine protein phosphatase PP1 to the nucleolus (By similarity). Involved in regulation of mRNA splicing. Inhibits SIPA1 GTPase activity. Involved in regulating expression of extracellular matrix genes. Associates with chromatin and may play a role in modulating chromatin structure (By similarity). B [...]