MeSH

The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.

A ubiquitous stress-responsive enzyme that catalyzes the oxidative cleavage of HEME to yield IRON; CARBON MONOXIDE; and BILIVERDIN.

Year introduced: 2006(1997)

A mixed function oxidase enzyme which during hemoglobin catabolism catalyzes the degradation of heme to ferrous iron, carbon monoxide and biliverdin in the presence of molecular oxygen and reduced NADPH. The enzyme is induced by metals, particularly cobalt.

Year introduced: 1998

Metalloproteins that contain a HEME ligand as the prosthetic group.

Year introduced: 2020(1984)

A dsRNA-activated cAMP-independent protein serine/threonine kinase that is induced by interferon. In the presence of dsRNA and ATP, the kinase autophosphorylates on several serine and threonine residues. The phosphorylated enzyme catalyzes the phosphorylation of the alpha subunit of EUKARYOTIC INITIATION FACTOR-2, leading to the inhibition of protein synthesis.

Year introduced: 1998

An autosomal dominant porphyria that is due to a deficiency of FERROCHELATASE (heme synthetase) in both the LIVER and the BONE MARROW, the last enzyme in the 8-enzyme biosynthetic pathway of HEME. Clinical features include mainly neurological symptoms, rarely cutaneous lesions, and elevated levels of protoporphyrin and COPROPORPHYRINS in the feces.

Year introduced: 2005

Proteins, usually acting in oxidation-reduction reactions, containing iron but no porphyrin groups. (Lehninger, Principles of Biochemistry, 1993, pG-10)

Year introduced: 1997

macromolecular heme binder found in human & porcine intestinal brush borders; HxuA, HxuB, and HxuC are heme:hemopexin complex-binding proteins from Haemophilus influenzae; ShuA is a Shigella dysenteriae type 1 heme receptor

Date introduced: February 6, 1981

Proteins that contain an iron-porphyrin, or heme, prosthetic group resembling that of hemoglobin. (From Lehninger, Principles of Biochemistry, 1982, p480)

Year introduced: 1973

together with HO-1, catalyzes the cleavage of heme to produce biliverdin IXalpha, CO & Fe; constitutively expressed in many mammalian tissues; not induced by inducers of heme oxygenase-1; has been sequenced

Date introduced: April 23, 1997

corresponds to residues 11 to 21 of cytochrome c bound to ferriheme; has peroxidase activity; amino acid sequence in Exp Eye Res 1997 Oct;65(4):457-70

Date introduced: January 1, 1977

A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite.

Year introduced: 1977

Cytochromes (electron-transporting proteins) with protoheme (HEME B) as the prosthetic group.

Year introduced: 2004(1983)

heme-containg peptide obtained by the proteolytic fragmentation of cytochrome c; inhibits lipid peroxidation

Date introduced: August 15, 1985

MW 400,000; from bovine erythrocytes

Date introduced: January 21, 1983

Cytochromes (electron-transporting proteins) in which the heme prosthetic group is heme a, i.e., the iron chelate of cytoporphyrin IX. (From Enzyme Nomenclature, 1992, p539)

Year introduced: 2004(1994)

A mitochondrial enzyme found in a wide variety of cells and tissues. It is the final enzyme in the 8-enzyme biosynthetic pathway of HEME. Ferrochelatase catalyzes ferrous insertion into protoporphyrin IX to form protoheme or heme. Deficiency in this enzyme results in ERYTHROPOIETIC PROTOPORPHYRIA.

Year introduced: 1991(1977)

RefSeq NM_026740

Date introduced: February 6, 2007

RefSeq NM_080669

Date introduced: November 2, 2005

an artificial O2 carrier that can transport O2 like hemoglobin; a recombinant human serum albumin (rHSA) incorporating synthetic heme with a covalently linked proximal base; structure in first source

Date introduced: June 29, 2005