A human protein hydroxylase that accepts D-residues
نویسندگان
چکیده
منابع مشابه
Genetic evidence that the human CYP2R1 enzyme is a key vitamin D 25-hydroxylase.
The synthesis of bioactive vitamin D requires hydroxylation at the 1 alpha and 25 positions by cytochrome P450 enzymes in the kidney and liver, respectively. The mitochondrial enzyme CYP27B1 catalyzes 1 alpha-hydroxylation in the kidney but the identity of the hepatic 25-hydroxylase has remained unclear for >30 years. We previously identified the microsomal CYP2R1 protein as a potential candida...
متن کاملMcLachlan Accepts Tulane Post
-In view of the relatively poor prognosis for patients after surgery for locally invasive colorectal cancer a trial of repeated systemic infusions of Corynebacterium parvum (CP) has been carried out. It is in this group of patients, with a high risk of recurrence from small residues of cancer left by the surgeon, that immunotherapy should have its optimum chance of success. A total of 92 patien...
متن کاملHomology between a prolyl hydroxylase subunit and a tissue protein that crossreacts immunologically with the enzyme.
A protein, enzymatically inactive but immunologically related to prolyl hydroxylase (prolyl-glycyl-peptide, 2-oxoglutarate:oxygen oxidoreductase; EC 1.14.11.2) (cross-reacting protein), has been purified to near homogeneity from skin of newborn rats. The purified protein has a molecular weight of 60,000 on gel filtration and sodium dodecyl sulfate gel electrophoresis, corresponding to that of t...
متن کاملResidues that affect human Argonaute2 concentration in cytoplasmic processing bodies.
Sequence-specific gene silencing triggered by double-stranded RNA is a fundamental gene regulatory mechanism present in almost all eukaryotes. Argonaute2 (Ago2) is the central protein component of RNA-induced silencing complex (RISC), and resides in cytoplasmic processing bodies (P-bodies). In the present study, we demonstrated one human mutant Ago2 protein containing 6 point mutations (G32W, F...
متن کاملIntroducing critical residues in the human prion protein and its Asp 178 Asn mutant by molecular dynamics simulation
The molecular dynamics (MD) simulation method is used to assess structural details for humanprion protein (hereafter PrPN) and its Asp178 Asn mutant (hereafter PrPm) which causes fatalfamilial insomnia disease. The results reveal that the flexibility and instability increase in PrPmcould be related to specific amino acids exposed to the solvent. Solvation free energy of PrPm is 20kjmot1nni2 mor...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Communications Chemistry
سال: 2020
ISSN: 2399-3669
DOI: 10.1038/s42004-020-0290-5