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Heme (American English), or haem (Commonwealth English, both pronounced /hi:m/ HEEM), is a ring-shaped iron-containing molecular component of hemoglobin, which is necessary to bind oxygen in the bloodstream. It is composed of four pyrrole rings with 2 vinyl and 2 propionic acid side chains. [1] Heme is biosynthesized in both the bone marrow and ...
Heme is a major source of dietary iron in humans and other mammals, and its synthesis in the body is well understood, but heme pathways are not as well understood. It is likely that heme is tightly regulated for two reasons: the toxic nature of iron in cells, and the lack of a regulated excretory system for excess iron.
Siroheme (or sirohaem) is a heme-like prosthetic group at the active sites of some enzymes to accomplish the six-electron reduction of sulfur and nitrogen. [1] It is a cofactor at the active site of sulfite reductase , which plays a major role in sulfur assimilation pathway, converting sulfite into sulfide , which can be incorporated into the ...
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12892 Ensembl n/a ENSMUSG00000022742 UniProt P36551 P36552 RefSeq (mRNA) NM_000097 NM_007757 RefSeq (protein) NP_000088 NP_031783 Location (UCSC) n/a Chr 16: 58.49 – 58.54 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Protein family Coprogen oxidase coproporphyrinogen iii oxidase from leishmania major Identifiers Symbol Coprogen oxidase Pfam PF01218 InterPro IPR001260 PROSITE ...
Summary of heme B biosynthesis—note that some reactions occur in the cytoplasm and some in the mitochondrion (yellow) Ferrochelatase catalyzes the insertion of ferrous iron into protoporphyrin IX in the heme biosynthesis pathway to form heme B. The enzyme is localized to the matrix-facing side of the inner mitochondrial membrane.
The number of heme C units bound to a holoprotein is highly variable. For vertebrate cells one heme C per protein is the rule but for bacteria this number is often 2, 4, 5, 6 or even 16 heme C groups per holoprotein. It is generally agreed the number and arrangement of heme C groups are related and even required for proper holoprotein function.
Tryptophan 2,3-dioxygenase is a heme-containing cytosolic enzyme encoded by gene TDO2. [5] Crystallographic studies of Xanthomonas campestris TD) [13] and Ralstonia metallidurans TDO) [16] have revealed that their structures are essentially identical and are intimately associated homotetrameric enzymes. [17]