WebJan 10, 2024 · Crystal Structure Of Human NADH-Cytochrome B5 Reductase WebMethemoglobinemia due to NADH-cytochrome b5 reductase deficiency is an autosomal recessive disorder characterized clinically by decreased oxygen carrying capacity of the blood, with resultant cyanosis and hypoxia (review by Percy and Lappin, 2008 ). There are 2 types of methemoglobin reductase deficiency.
METHEMOGLOBINEMIA DUE TO DEFICIENCY OF METHEMOGLOBIN REDUCTASE
WebMar 9, 2024 · cytochrome b, mitochondrial provided by MGI Primary source MGI:MGI:102501 Gene type Lineage Also known as Summary Predicted to enable metal ion binding activity and ubiquinol-cytochrome-c reductase activity. WebMay 24, 2005 · Plasma membrane reductase that uses cytoplasmic ascorbate as an electron donor to reduce extracellular Fe 3+ into Fe 2+ ( PubMed: 30272000 ). Probably functions in dietary iron absorption at the brush border of duodenal enterocytes by producing Fe 2+, the divalent form of iron that can be transported into enterocytes ( PubMed: … biodata background images
Crystals Free Full-Text Amino Acid Substitutions in the Non …
WebSuperoxide anion production and cytochrome c reduction are the consequences of the stimulated NADH consumption by cytochrome b 5 reductase upon complex formation with cytochrome c and suggest a major role of this enzyme as … Cytochrome-b5 reductase is a NADH-dependent enzyme that converts ferricytochrome from a Fe3+ form to a Fe2+ form. It contains FAD and catalyzes the reaction: In its b5-reducing capacity, this enzyme is involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, and drug … See more • Cytochrome b5 • Diaphorase • Methemoglobinemia • Reductase • Leghemoglobin reductase See more • Cytochrome-B(5)+Reductase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) See more WebCytochrome b5 deficiency is a rare condition and form of isolated 17,20-lyase deficiency caused by deficiency in cytochrome b 5, a small hemoprotein that acts as an allosteric factor to facilitate the interaction of CYP17A1 (17α-hydroxylase/17,20-lyase) with P450 oxidoreductase (POR), thereby allowing for the 17,20-lyase activity of CYP17A1. dahlgren backpack campground