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Literature summary extracted from

  • Schubert, H.L.; Raux, E.; Brindley, A.A.; Leech, H.K.; Wilson, K.S.; Hill, C.P.; Warren, M.J.
    The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase (2002), EMBO J., 21, 2068-2075.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.1.76
-
 Saccharomyces cerevisiae
4.99.1.4 MET8 gene Saccharomyces cerevisiae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.1.76 space group C2, a : 156.1 A,b : 81.2 A, c : 104.2 A Saccharomyces cerevisiae
4.98.1.1 in complex with beta-NAD+ Saccharomyces cerevisiae
4.99.1.4 X-ray crystal structure of Met8p, hanging drop method Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
1.3.1.76 D141A site-directed mutagenesis Saccharomyces cerevisiae
1.3.1.76 G22D site-directed mutagenesis Saccharomyces cerevisiae
1.3.1.76 H237A site-directed mutagenesis Saccharomyces cerevisiae
4.98.1.1 D141A no enzymic activity, no dehydrogenase activity Saccharomyces cerevisiae
4.98.1.1 G22D wild type enzymic activity, no dehydrogenase activity Saccharomyces cerevisiae
4.98.1.1 H237A retains both enzymic and dehydrogenase activity Saccharomyces cerevisiae
4.99.1.4 D141A mutant of bifunctional Met8p is completely inactive as both dehydrogenase and ferrochelatase Saccharomyces cerevisiae
4.99.1.4 G22D mutant of bifunctional Met8p is completely inactive as dehydrogenase, but functions as ferrochelatase Saccharomyces cerevisiae
4.99.1.4 H237A mutant of bifunctional Met8p is active as both dehydrogenase and ferrochelatase Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.1.76 precorrin-2 + NAD+ Saccharomyces cerevisiae
-
 sirohydrochlorin + NADH + H+
-
 ?
1.3.1.76 precorrin-2 + NAD+ Saccharomyces cerevisiae bifunctional dehydrogenase and ferrochelatase, second of three steps leading to formation of siroheme from uroporphyrinogen III sirohydrochlorin + NADH + H+
-
 ?
4.99.1.4 sirohydrochlorin + Fe2+ Saccharomyces cerevisiae
-
 siroheme + H+
-
 ?
4.99.1.4 sirohydrochlorin + Fe2+ Saccharomyces cerevisiae Met8p catalyzes the final two steps in the biosynthesis of siroheme involving a beta-NAD+-dependent dehydrogenation of precorrin-2 to generate sirohydrochlorin followed by ferrochelation to yield siroheme siroheme + 2 H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.76 Saccharomyces cerevisiae P15807
-
-
1.3.1.76 Saccharomyces cerevisiae P15807 yeast
-
4.98.1.1 Saccharomyces cerevisiae
-
 bifunctional dehydrogenase and ferrochelatase
-
4.99.1.4 Saccharomyces cerevisiae
-
-
-
4.99.1.4 Saccharomyces cerevisiae P15807
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.1.76
-
 Saccharomyces cerevisiae
4.99.1.4 recombinant Met8p Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3.1.76 0.0112
-
 wild-type Saccharomyces cerevisiae
1.3.1.76 0.0133
-
 mutant H237A Saccharomyces cerevisiae
4.99.1.4 additional information
-
-
 Saccharomyces cerevisiae
4.99.1.4 0.0311
-
 wild-type Met8p Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.76 precorrin-2 + NAD+
-
 Saccharomyces cerevisiae sirohydrochlorin + NADH + H+
-
 ?
1.3.1.76 precorrin-2 + NAD+ bifunctional dehydrogenase and ferrochelatase, second of three steps leading to formation of siroheme from uroporphyrinogen III Saccharomyces cerevisiae sirohydrochlorin + NADH + H+
-
 ?
4.99.1.4 sirohydrochlorin + Co2+
-
 Saccharomyces cerevisiae cobalt-sirohydrochlorin + 2 H+
-
 ?
4.99.1.4 sirohydrochlorin + Fe2+
-
 Saccharomyces cerevisiae siroheme + H+
-
 ?
4.99.1.4 sirohydrochlorin + Fe2+ Met8p structure, bifunctional Met8p catalyzes the final two steps in the biosynthesis of siroheme involving a beta-NAD+-dependent dehydrogenation of precorrin-2 to generate sirohydrochlorin followed by ferrochelation to yield siroheme, both catalytic activities share a single active site, Asp-141 functions as a general base and plays an essential role in both dehydrogenase and chelatase processes Saccharomyces cerevisiae siroheme + 2 H+
-
 ?
4.99.1.4 sirohydrochlorin + Fe2+ Met8p catalyzes the final two steps in the biosynthesis of siroheme involving a beta-NAD+-dependent dehydrogenation of precorrin-2 to generate sirohydrochlorin followed by ferrochelation to yield siroheme Saccharomyces cerevisiae siroheme + 2 H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.1.76 homodimer
-
 Saccharomyces cerevisiae
4.99.1.4 homodimer three structural domains per monomer, domain structure Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
1.3.1.76 Met8p
-
 Saccharomyces cerevisiae
4.99.1.4 Met8p Saccharomyces cerevisiae Saccharomyces cerevisiae
4.99.1.4 More Met8p is a class 2 chelatase Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.99.1.4 8
-
 assay at Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.76 NAD+ beta-NAD+-dependent dehydrogenation of precorrin-2 Saccharomyces cerevisiae