Biomaterial Database

The biosynthesis of uroporphyrinogen III: order of assembly of the four porphobilinogen molecules in the formation of the tetrapyrrole ring. 1979

P M Jordan, and J S Seehra

UI	MeSH Term	Description	Entries
D011163	Hydroxymethylbilane Synthase	An enzyme that catalyzes the tetrapolymerization of the monopyrrole PORPHOBILINOGEN into the hydroxymethylbilane preuroporphyrinogen (UROPORPHYRINOGENS) in several discrete steps. It is the third enzyme in the 8-enzyme biosynthetic pathway of HEME. In humans, deficiency in this enzyme encoded by HMBS (or PBGD) gene results in a form of neurological porphyria (PORPHYRIA, ACUTE INTERMITTENT). This enzyme was formerly listed as EC 4.3.1.8	Porphobilinogen Ammonia-Lyase,Porphobilinogen Deaminase,Uroporphyrinogen I Synthase,Hydroxymethylbilane Synthetase,Pre-uroporphyrinogen Synthetase,Preuroporphyrinogen Synthetase,Ammonia-Lyase, Porphobilinogen,Deaminase, Porphobilinogen,Porphobilinogen Ammonia Lyase,Pre uroporphyrinogen Synthetase,Synthase, Hydroxymethylbilane,Synthase, Uroporphyrinogen I,Synthetase, Hydroxymethylbilane,Synthetase, Pre-uroporphyrinogen,Synthetase, Preuroporphyrinogen
D011165	Porphyrinogens	Colorless reduced precursors of porphyrins in which the pyrrole rings are linked by methylene (-CH2-) bridges.
D002250	Carbon Radioisotopes	Unstable isotopes of carbon that decay or disintegrate emitting radiation. C atoms with atomic weights 10, 11, and 14-16 are radioactive carbon isotopes.	Radioisotopes, Carbon
D003304	Coproporphyrinogen Oxidase	An enzyme that catalyzes the oxidative decarboxylation of coproporphyrinogen III to protoporphyrinogen IX by the conversion of two propionate groups to two vinyl groups. It is the sixth enzyme in the 8-enzyme biosynthetic pathway of HEME, and is encoded by CPO gene. Mutations of CPO gene result in HEREDITARY COPROPORPHYRIA.	Coproporphyrinogenase,Coproporphyrinogen III Oxidases,III Oxidases, Coproporphyrinogen,Oxidase, Coproporphyrinogen,Oxidases, Coproporphyrinogen III
D000623	Porphobilinogen Synthase	An enzyme that catalyzes the formation of porphobilinogen from two molecules of 5-aminolevulinic acid. EC 4.2.1.24.	Aminolevulinate Hydro-Lyase,Aminolevulinic Acid Dehydratase,ALA-Dehydrase,delta-Aminolevulinate Dehydratase,delta-Aminolevulinic Acid Dehydratase,ALA Dehydrase,Acid Dehydratase, Aminolevulinic,Acid Dehydratase, delta-Aminolevulinic,Aminolevulinate Hydro Lyase,Dehydratase, Aminolevulinic Acid,Dehydratase, delta-Aminolevulinate,Dehydratase, delta-Aminolevulinic Acid,Hydro-Lyase, Aminolevulinate,Synthase, Porphobilinogen,delta Aminolevulinate Dehydratase,delta Aminolevulinic Acid Dehydratase
D012242	Rhodobacter sphaeroides	Spherical phototrophic bacteria found in mud and stagnant water exposed to light.	Rhodopseudomonas sphaeroides,Rhodobacter spheroides,Rhodopseudomonas spheroides
D014575	Uroporphyrinogen Decarboxylase	An enzyme that catalyzes the decarboxylation of UROPORPHYRINOGEN III to coproporphyrinogen III by the conversion of four acetate groups to four methyl groups. It is the fifth enzyme in the 8-enzyme biosynthetic pathway of HEME. Several forms of cutaneous PORPHYRIAS are results of this enzyme deficiency as in PORPHYRIA CUTANEA TARDA; and HEPATOERYTHROPOIETIC PORPHYRIA.	Uroporphyrinogen Carboxy-Lyase,Uroporphyrinogen III Decarboxylase,Carboxy-Lyase, Uroporphyrinogen,Decarboxylase, Uroporphyrinogen,Decarboxylase, Uroporphyrinogen III,Uroporphyrinogen Carboxy Lyase
D014576	Uroporphyrinogen III Synthetase	An enzyme that catalyzes the cyclization of hydroxymethylbilane to yield UROPORPHYRINOGEN III and water. It is the fourth enzyme in the 8-enzyme biosynthetic pathway of HEME, and is encoded by UROS gene. Mutations of UROS gene result in CONGENITAL ERYTHROPOIETIC PORPHYRIA.	Cosynthase,Uroporphyrinogen III Cosynthetase,Uroporphyrinogen Isomerase,Uroporphyrinogen-III Synthase,Cosynthetase, Uroporphyrinogen III,Isomerase, Uroporphyrinogen,Synthase, Uroporphyrinogen-III,Synthetase, Uroporphyrinogen III,Uroporphyrinogen III Synthase
D014577	Uroporphyrinogens	Porphyrinogens which are intermediates in heme biosynthesis. They have four acetic acid and four propionic acid side chains attached to the pyrrole rings. Uroporphyrinogen I and III are formed from polypyrryl methane in the presence of uroporphyrinogen III cosynthetase and uroporphyrin I synthetase, respectively. They can yield uroporphyrins by autooxidation or coproporphyrinogens by decarboxylation.	Uroporphyrinogen III