Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Schubert, H.L.; Raux, E.; Matthews, M.A.; Phillips, J.D.; Wilson, K.S.; Hill, C.P.; Warren, M.J.
    Structural diversity in metal ion chelation and the structure of uroporphyrinogen III synthase (2002), Biochem. Soc. Trans., 30, 595-600.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.99.1.3
-
 Salmonella enterica subsp. enterica serovar Typhimurium
4.99.1.4 X-ray crystal structure of Met8p Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.75 additional information 16 known mutations causing congenital erythropoietic porphyria in humans via alterations of the tertiary enzyme structure Homo sapiens
4.99.1.4 D141A mutant of bifunctional Met8p is devoid of both dehydrogenase and ferrochelatase activities Saccharomyces cerevisiae
4.99.1.4 G22D mutant of bifunctional Met8p is completely inactive as NAD+-dependent dehydrogenase, but functions as ferrochelatase Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.99.1.3 Co2+ incorporates Co2+ over Fe2+ Salmonella enterica subsp. enterica serovar Typhimurium

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.75 28000
-
 about Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.75 hydroxymethylbilane Homo sapiens macrocyclic, role of the enzyme in tetrapyrrole based copound biosynthesis, overview uroporphyrinogen-III + H2O
-
 ?
4.99.1.3 precorrin-2 + Co2+ Salmonella enterica subsp. enterica serovar Typhimurium tetrapyrrole biosynthesis, formation of tetrapyrrole cofactors Co-precorrin-2 + H+
-
 ?
4.99.1.4 sirohydrochlorin + Fe2+ Saccharomyces cerevisiae Met8p catalyzes ferrochelation during the biosynthesis of siroheme siroheme + 2 H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.75 Homo sapiens
-
-
-
4.99.1.3 Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-
4.99.1.4 Saccharomyces cerevisiae
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.1.75 hydroxymethylbilane = uroporphyrinogen III + H2O in the presence of hydroxymethylbilane synthase EC 4.3.1.8, enzyme forms uroporphyrinogen III from porphobilinogen, reaction mechanism, does not require acid/base catalysis, active site structure Homo sapiens
a
4.99.1.4 siroheme + 2 H+ = sirohydrochlorin + Fe2+ the enzyme from Pseudomonas chloroaphis contains Ca2+ and protoheme IX, the iron of which must be in the form Fe2+ for activity, the enzyme exhibits a strong preference for aliphatic aldoximes, such as butyraldoxime and acetaldoxime, over aromatic aldoximes, such as pyridine-2-aldoxime, which is a poor substrate, no activity was found with the aromatic aldoximes benzaldoxime and pyridine-4-aldoxime, mechanism Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.75 hydroxymethylbilane linear tetrapyrrole Homo sapiens uroporphyrinogen-III + H2O
-
 ?
4.2.1.75 hydroxymethylbilane macrocyclic, role of the enzyme in tetrapyrrole based copound biosynthesis, overview Homo sapiens uroporphyrinogen-III + H2O
-
 ?
4.99.1.3 precorrin-2 + Co2+
-
 Salmonella enterica subsp. enterica serovar Typhimurium Co-precorrin-2 + H+
-
 ?
4.99.1.3 precorrin-2 + Co2+ tetrapyrrole biosynthesis, formation of tetrapyrrole cofactors Salmonella enterica subsp. enterica serovar Typhimurium Co-precorrin-2 + H+
-
 ?
4.99.1.4 sirohydrochlorin + Fe2+ Met8p catalyzes ferrochelation during the synthesis of siroheme, both ferrochelation and NAD+-dependent dehydrogenation of preccorin-2 to produce sirohydrochlorin take place in a single bifunctional active site, Asp-141 participates in both catalytic reactions, which are not linked mechanistically, mechanism Saccharomyces cerevisiae siroheme + 2 H+
-
 ?
4.99.1.4 sirohydrochlorin + Fe2+ Met8p catalyzes ferrochelation during the biosynthesis of siroheme Saccharomyces cerevisiae siroheme + 2 H+
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.75 More enzyme structure, model Homo sapiens
4.99.1.4 homodimer each monomer is composed of three functional domains, domain structure Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
4.2.1.75 U3S
-
 Homo sapiens
4.2.1.75 Uroporphyrinogen III synthase
-
 Homo sapiens
4.99.1.3 anaerobic cobalt chelatase
-
 Salmonella enterica subsp. enterica serovar Typhimurium
4.99.1.3 CbiK
-
 Salmonella enterica subsp. enterica serovar Typhimurium
4.99.1.3 cobalt chelatase
-
 Salmonella enterica subsp. enterica serovar Typhimurium
4.99.1.4 Met8p Saccharomyces cerevisiae Saccharomyces cerevisiae
4.99.1.4 More member of the class 2 chelatases Saccharomyces cerevisiae