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CYP2U1 encodes a member of the cytochrome P450 superfamily of enzymes. Additionally we are shipping Cytochrome P450, Family 2, Subfamily U, Polypeptide 1 Proteins (3) and Cytochrome P450, Family 2, Subfamily U, Polypeptide 1 Kits (2) and many more products for this protein.
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Most CYP2U1 missense mutations in hereditary spastic paraplegia 56 lead to an inhibition of enzymatic activity that can be explained by the loss of proper heme binding to the protein or modification in protein structure.
we report a patient with SPG56 with novel compound heterozygous mutations in CYP2U1 which were identified by whole exome sequencing. Our patient exhibited complex features together with delayed myelination, broadening the phenotypic spectrum of SPG56, and implying that CYP2U1 should be screened in HSP with delayed myelination
the mode of interaction of several Fe(III)-heme ligands and substrates with the active site of CYP2U1 on the basis of spectroscopic and molecular docking data.[CYP2U1]
protein sequence of CYP2U1 displayed two unique characteristics when compared to those of the human CYPs, the presence of a longer N-terminal region upstream of the putative trans-membrane helix (TMH) containing 8 proline residues, and of an insert of about 20 amino acids containing 5 arginine residues between helices A' and A
Cytochrome P450 2U1 (CYP2U1) exhibits several distinctive characteristics among the 57 human CYPs, such as its presence in almost all living organisms with a highly conserved sequence, its particular gene organization with only five exons, its major location in thymus and brain, and its protein sequence involving an unusually long N-terminal region containing 8 proline residues. [review]
This is the first formal report of pigmentary degenerative maculopathy associated with a CYP2U1 homozygous mutation
we identified two novel mutations in CYP2U1 in two unrelated Hereditary spastic paraplegia patients by whole exome sequencing
This is the first report of CYP2E1 and CYP2U1 protein expression in human Amygdala.
Data suggest that the 3D model could be useful to identify other substrates of cytochrome P450 2U1 (CYP2U1) and help in understanding its physiologic roles.
The CYP2U1 gene shows a low mutation frequency in a general population of complicated hereditary spastic paraparesis
human cytochrome P450 2U1 oxidizes endogenous N-arachidonoylserotonin
CYP1B1 and CYP2U1 were the only quantifiable CYPs in in freshly isolated human brain microvessels.
Genetic polymorphism of CYP2U1, a cytochrome P450 involved in fatty acids hydroxylation.
CYP2U1 plays an important physiological role in fatty acid signaling processes in both cerebellum and thymus
This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This enzyme is a hydroxylase that metabolizes arachidonic acid, docosahexaenoic acid, and other long chain fatty acids.
cytochrome P450 2U1
, cytochrome P450, family 2, subfamily U, polypeptide 1
, spastic paraplegia 49
, cytochrome P450, 2u1