Involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. Catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin.
Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated pro-inflammatory responses. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of ARNTL/BMAL1 in the blood vessels.
Phosphopantothenoylcysteine Decarboxylase (PPC-DC) is an essential enzyme in the biosynthesis ofCoenzyme A and catalyzes the decarboxylation of PPC to Phosphopantetheine. PPC-DC catalyzes the decarboxylation of the Cysteine moiety of 4-Phosphopantothenoylcysteine (PPC) to form 4-Phosphopantetheine (PPantSH), this reaction forms part of the biosynthesis of Coenzyme A. The enzyme is a member of the larger family of Cysteine Decarboxylases including the Lantibiotic-Biosynthesizing enzymes EpiD and MrsD, all of which use a tightly bound Flavin cofactor to oxidize the Thiol moiety of the substrate to a Thioaldehyde.
PPIase is a member of the immunophilin protein family. It also belongs to the cyclophilin-type PPIase family; PPIL3 subfamily. PPIase contains 1 PPIase cyclophilin-type domain. Members of the immunophilin protein family play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. It has a very high substrate specificity for the four-residue peptide Ala-Ala-Pro-Phe only when the proline peptide bond is in the trans state. It interacts with several intracellular signal transduction proteins including type I TGF-beta receptor. It also interacts with multiple intracellular calcium release channels; and coordinates multi-protein complex formation of the tetrameric skeletal muscle ryanodine receptor. In mouse; deletion of this homologous gene causes congenital heart disorder known as noncompaction of left ventricular myocardium.
Peptidyl-Prolyl Cis-Trans Isomerase FKBP7 (FKBP7) is a member of the FKBP-type peptidyl-prolyl cis/trans isomerase (PPIase) family. FKBP7 contains two EF-hand domains and one PPIase FKBP-type domain. FKBP7 exhibits PPIase activity and function as molecular chaperones. In addition, FKBP7 accelerates the folding of proteins during protein synthesis. It has been shown that Hsp90 complex to the nucleus bind its PPIase domain to cytoplasmic dynein, the motor protein responsible for retrograde movement along microtubules.
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