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*  HMOX1
Heme oxygenase mediates the first step of heme catabolism, it cleaves heme to form biliverdin. Heme oxygenase, an essential ... Heme oxygenase occurs as 2 isozymes, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. HMOX1 and HMOX2 belong ... Heme oxygenase-1 deficiency The ability of oxygenase 1 to catabolize free heme and produce carbon monoxide (CO) gives its anti- ... HMOX1 (heme oxygenase (decycling) 1) is a human gene that encodes for the enzyme heme oxygenase 1 (EC 1.14.99.3). ...
*  Hemopexin
... binds heme with the highest affinity of any known protein. Its function is scavenging the heme released or lost by ... Heme released during oxidation of Hb to met-Hb or from heme saturated hepatocytes is bound by albumin and rapidly transferred ... an inhibitor of heme oxygenase. Role for hemopexin in hepatic uptake of Sn-protoporphyrin IX and induction of mRNA for heme ... "Regulation of heme oxygenase and metallothionein gene expression by the heme analogs, cobalt-, and tin-protoporphyrin". The ...
*  Hemozoin
A heme is a prosthetic group that consists of an iron atom contained in the center of a heterocyclic porphyrin ring. Free heme ... These drugs bind to both free heme and hemozoin crystals, and therefore block the addition of new heme units onto the growing ... Kikuchi G, Yoshida T, Noguchi M (December 2005). "Heme oxygenase and heme degradation". Biochem Biophys Res Commun. 338 (1): ... where an enzyme called heme oxygenase instead breaks excess heme into biliverdin, iron, and carbon monoxide. Several mechanisms ...
*  Iron deficiency
Following are two tables showing the richest foods in heme and non-heme iron. In both tables, food serving sizes may differ ... Iron from non-heme sources is more readily absorbed if consumed with foods that contain either heme-bound iron or vitamin C. ... Good sources of dietary iron have heme-iron, as this is most easily absorbed and is not inhibited by medication or other ... Non-heme sources do contain iron, though it has reduced bioavailability. Examples are lentils, beans, leafy vegetables, ...
*  Aminolevulinic acid
This protoporphyrin molecule chelates with iron in presence of enzyme ferrochelatase to produce Heme. Heme increases the ... Excess heme is converted in macrophages to Biliverdin and ferrous ions by the enzyme HO-1. Biliverdin formed further gets ... In humans, 5ALA is a precursor to heme. Biosynthesized, 5ALA goes through a series of transformations in the cytosol and ... Gardener, L.C., Cox, T.M. (1988). Biosynthesis of heme in immature erythroid cells. The Journal of Biological Chemistry, 263, ...
*  Zinc protoporphyrin
The chemical group that ZnPP belongs to is similar to free heme which is a natural substrate of heme oxygenase. ZnPP is known ... Some reports, for instance, measured the ZPP/Heme molar ratio (μmole ZPP per mole of heme), but reported this as the weight ... Instead of incorporating a ferrous ion, to form heme, protoporphyrin IX, the immediate precursor of heme, incorporates a zinc ... and leukemia all show a susceptibility to ZnPP due to increase expression of heme oxygenase. The inhibition of heme oxygenase ...
*  Heme oxygenase
... cleaves the heme ring at the alpha-methene bridge to form either biliverdin or, if the heme is still attached to ... Three isoforms of heme oxygenase are known. Heme oxygenase 1 (HO-1) is an inducible isoform in response to stress such as ... A third heme oxygenase (HO-3) is not catalytically active, but is thought to work in oxygen sensing.[citation needed] Heme ... Heme oxygenase or haem oxygenase (HO) is an enzyme that catalyzes the degradation of heme. This produces biliverdin, ferrous ...
*  Human iron metabolism
Heme iron in animals is from blood and heme-containing proteins in meat and mitochondria, whereas in plants, heme iron is ... Heme groups are also present in myoglobin to store and diffuse oxygen in muscle cells. The human body needs iron for oxygen ... To be absorbed, dietary iron can be absorbed as part of a protein such as heme protein or iron must be in its ferrous Fe2+ form ... Iron bound to proteins or cofactors such as heme is safe. Also, there are virtually no truly free iron ions in the cell, since ...
*  Aminolevulinic acid synthase
Since the enzyme appears to be located near its source of succinyl-CoA and the end of the heme pathway indicates that the ... ALAS1 and ALAS2 catalyze the first step in the process of heme synthesis. It is the first irreversible step and is also rate ... This means that the beginning of the formation of hemes is very intentional and subject to a variety of areas of feedback. For ... Aminolevulinic Acid Synthase Deficiency results in a lack of ability to create heme since its job is to catalyze the first step ...
*  Heme
The most common type is heme B; other important types include heme A and heme C. Isolated hemes are commonly designated by ... Heme S is related to heme B by having a formal group at position 2 in place of the 2-vinyl group. Heme S is found in the ... Heme m is the derivative of heme B covalently bound at the active site of peroxide. Heme m contains the two ester bonds at the ... Rae, T.; Goff, H. (1998). "The heme prosthetic group of lactoperoxidase. Structural characteristics of heme l and heme l- ...
*  Heme O
... (or haem O) differs from the closely related heme A by having a methyl group at ring position 8 instead of the formyl ... Heme O, found in the bacterium Escherichia coli, functions in a similar manner to heme A in mammalian oxygen reduction. Myles R ... Heme o3 and CuB(II) in Escherichia coli Quinol Oxidase, Cytochrome bo3: MCD and EPR Studies". J. Am. Chem. Soc. 126: 4157-4166 ...
*  Heme arginate
... (or haem arginate) is a compound of heme and arginine used in the treatment of acute porphyrias. This heme ... Heme arginate is a heme compound, whereby L-arginine is added to prevent rapid degradation. It is given intravenously, and its ... Volin, L; V Rasi; E Vahtera; R Tenhunen (1988). "Heme arginate: effects on hemostasis" (PDF). Blood. 71: 625-628. Retrieved 28 ...
*  Heme ligase
... (EC 4.99.1.8, heme detoxification protein, HDP, hemozoin synthase) is an enzyme with systematic name Fe3+: ... Heme ligase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology portal. ... beta-hematin This heme detoxifying enzyme is found in Plasmodium parasites. Jani, D.; Nagarkatti, R.; Beatty, W.; Angel, R.; ... Slebodnick, C.; Andersen, J.; Kumar, S.; Rathore, D. (2008). "HDP-a novel heme detoxification protein from the malaria parasite ...
*  Heme C
... (or haem C) is an important kind of heme. The correct structure of heme C was published, in mid 20th century, by the ... Heme C differs from heme B in that the two vinyl side chains of heme B are replaced by covalent, thioether linkages to the ... CS1 maint: Multiple names: authors list (link) Heme Protoporphyrin IX Heme A Heme B Hemeprotein. ... The structure of heme C, based upon NMR and IR experiments of the reduced, Fe(II), form of the heme, was confirmed in 1975. The ...
*  Heme B
... or haem B (also known as protoheme IX) is the most abundant heme. Hemoglobin and myoglobin are examples of oxygen ... The correct structures of heme B and heme S were first elucidated by German chemist Hans Fischer. Fischer, H.; Orth, H. (1934 ... also contain heme B at one of two active sites. Generally, heme B is attached to the surrounding protein matrix (known as the ... transport proteins that contain heme B. The peroxidase family of enzymes also contain heme B. The COX-1 and COX-2 enzymes ( ...
*  Heme A
... is similar to heme o, in that both have this farnesyl addition at position 2 but heme O does not have the formyl group ... Like heme B, heme A is often attached to the apoprotein through a coordinate bond between the heme iron and a conserved amino ... is a structural relative of heme B, a component of hemoglobin, the red pigment in blood. Heme A differs from heme B in that a ... Heme A (or haem A) is a heme, a coordination complex consisting of a macrocyclic ligand called a porphyrin, chelating an iron ...
*  Heme-transporting ATPase
... and heme, whereas its 3 products are ADP, phosphate, and heme. This enzyme belongs to the family of hydrolases, specifically ... In enzymology, a heme-transporting ATPase (EC 3.6.3.41) is an enzyme that catalyzes the chemical reaction ATP + H2O + hemein ... Jekabsons W, Schuster W (1995). "orf250 encodes a second subunit of an ABC-type heme transporter in Oenothera mitochondria". ... The systematic name of this enzyme class is ATP phosphohydrolase (heme-exporting). This enzyme participates in abc transporters ...
*  Animal heme-dependent peroxidases
... is a family of peroxidases. Peroxidases are found in bacteria, fungi, plants and animals. On ... Poulos TL, Li H (1994). "Structural variation in heme enzymes: a comparative analysis of peroxidase and P450 crystal structures ... at the heme binding site. Both MPO and the catalytic domain of PGHS are mainly alpha-helical, 19 helices being identified as ... the basis of sequence similarity, a number of animal heme peroxidases can be categorized as members of a superfamily: ...
*  Nari Mela Kake Heme
Nari (Kurdish: Narî) (1874-1944) is the pen name for Narî Mele Kekê Hemê, a Kurdish poet. He was born and died in Marivan. He had a close relationship to Mahmud Barzanji, Taher Begi Jaf and Qani. Nari wrote lyric and mystic poems in Kurdish and Persian. The bulk of his poems are in the form of ghazal. He was mostly influenced by Nalî and Mahwi among Kurdish poets and by Hafez among Persian poets. Sajjadi Ala'edin (1951), The history of Kurdish literature, Ma'aref, Baghdad. Khazanedar, Maroof (2002), The history of Kurdish literature, Aras, Erbil ...
*  Vitamin B6
"Heme Synthesis". RPI.edu. doi:10.1042/BJ20030513. Retrieved 2012-11-02. McCormick, D. B. (2006). "Vitamin B6". In Bowman, B. A ... due to impaired heme synthesis). Less severe cases present with metabolic disease[clarify] associated with insufficient ...
*  Cytochrome
... to visible spectroscopic signatures of hemes are still used to identify heme type from the reduced bis-pyridine-ligated state, ... The heme group is a highly conjugated ring system (which allows its electrons to be very mobile) surrounding a metal ion, which ... Reedy, C. J.; Gibney, B. R. (February 2004). "Heme protein assemblies". Chem Rev. 104 (2): 617-49. doi:10.1021/cr0206115. PMID ... Cytochromes are iron containing hemeproteins central to which are heme groups that are primarily responsible for the generation ...
*  Dioxygenase
... which are heme dioxygenases that utilize iron coordinated by a heme B prosthetic group. While these dioxygenases are of ... and those utilizing a heme prosthetic group. The mononuclear iron dioxygenases, or non-heme iron-dependent dioxygenases as they ... The other heme iron-dependent dioxygenase, IDO, also has relevance to human health, as it functions in inflammatory responses ... While most iron-dependent dioxygenases utilize a non-heme iron cofactor, the oxidation of L-(and D-)tryptophan to N- ...
*  Tryptophan 2,3-dioxygenase
TDO is assumed to react in the same way, but a ferryl heme has not been observed in TDO. See also discussion of mechanism for ... In enzymology, tryptophan 2,3-dioxygenase (EC 1.13.11.11) is a heme enzyme that catalyzes the oxidation of L-tryptophan (L-Trp ... This suggested a base-catalysed abstraction mechanism, involving only the ferrous FeII) heme. It is assumed that TDO and IDO ... In IDO, a ferryl heme (FeIV) has been identified during turnover. Mechanistic proposals have therefore been adjusted to include ...
*  Fliflet/Hamre
"Heme" Official Website. ...
*  Lesser Poland
"About Kraków". Heme Oxygenases 2007 Conference. Jagiellonian University. Archived from the original on 15 July 2007. Retrieved ...