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Literature summary for 4.99.1.4 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
Search for more literature for 4.99.1.4

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray crystal structure of Met8p Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
D141A mutant of bifunctional Met8p is devoid of both dehydrogenase and ferrochelatase activities Saccharomyces cerevisiae
G22D mutant of bifunctional Met8p is completely inactive as NAD+-dependent dehydrogenase, but functions as ferrochelatase Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
sirohydrochlorin + Fe2+ Saccharomyces cerevisiae Met8p catalyzes ferrochelation during the biosynthesis of siroheme siroheme + 2 H+
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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+
-
 ?
sirohydrochlorin + Fe2+ Met8p catalyzes ferrochelation during the biosynthesis of siroheme Saccharomyces cerevisiae siroheme + 2 H+
-
 ?

Subunits

Subunits Comment Organism
homodimer each monomer is composed of three functional domains, domain structure Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
Met8p Saccharomyces cerevisiae Saccharomyces cerevisiae
More member of the class 2 chelatases Saccharomyces cerevisiae