Biomaterial Database

Uroporphyrinogen III, an intermediate in the biosynthesis of the nickel-containing factor F430 in Methanobacterium thermoautotrophicum. 1983

H Gilles, and R K Thauer

Factor F430 is a nickel-containing porphinoid present in methanogenic bacteria. The synthesis of this nickel tetrapyrrole from 5-aminolevulinic acid was studied in Methanobacterium thermoautotrophicum. This anaerobic archaebacterium was found to accumulate [14C]uroporphyrinogen III (1.8 mumol/g) when growing on nickel-free medium (less than 50 nmol/l) supplemented with 2 mM 5-amino-[14C]levulinic acid. The accumulated urophorphyrinogen III was quantitatively converted to factor F430 when the cells were incubated in aminolevulinate-free medium with 5 microM NiCl2. The newly synthesized factor had the same specific radioactivity as the precursor uroporphyrinogen III. These findings indicate that the nickelporphinoid is biosynthetically derived from uroporphyrinogen III. The presence and some properties of the enzymes catalyzing the synthesis of uroporphyrinogen III from 5-aminolevulinic acid in M. thermoautotrophicum are also described.

UI	MeSH Term	Description	Entries
D008665	Metalloporphyrins	Porphyrins which are combined with a metal ion. The metal is bound equally to all four nitrogen atoms of the pyrrole rings. They possess characteristic absorption spectra which can be utilized for identification or quantitative estimation of porphyrins and porphyrin-bound compounds.	Metalloporphyrin
D008667	Metalloproteins	Proteins that have one or more tightly bound metal ions forming part of their structure. (Dorland, 28th ed)	Metalloprotein
D009532	Nickel	A trace element with the atomic symbol Ni, atomic number 28, and atomic weight 58.69. It is a cofactor of the enzyme UREASE.
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.
D000622	Aminolevulinic Acid	A compound produced from succinyl-CoA and GLYCINE as an intermediate in heme synthesis. It is used as a PHOTOCHEMOTHERAPY for actinic KERATOSIS.	5-Amino Levulinic Acid,5-Aminolaevulinate,5-Aminolevulinate,Aminolevulinic Acid Hydrochloride,Delta-Aminolevulinic Acid,Levulan,5 Amino Levulinic Acid,5 Aminolaevulinate,5 Aminolevulinate,Acid Hydrochloride, Aminolevulinic,Acid, 5-Amino Levulinic,Acid, Aminolevulinic,Acid, Delta-Aminolevulinic,Delta Aminolevulinic Acid,Hydrochloride, Aminolevulinic Acid,Levulinic Acid, 5-Amino
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
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
D019605	Euryarchaeota	A phylum of ARCHAEA comprising at least seven classes: Methanobacteria, Methanococci, Halobacteria (extreme halophiles), Archaeoglobi (sulfate-reducing species), Methanopyri, and the thermophiles: Thermoplasmata, and Thermococci.	Archaeoglobi,Halobacteria,Methanoococci,Methanopyri,Thermococci,Thermoplasmata,Methanobacteria