BRENDA - Enzyme Database show
show all sequences of 4.99.1.4

The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase

Schubert, H.L.; Raux, E.; Brindley, A.A.; Leech, H.K.; Wilson, K.S.; Hill, C.P.; Warren, M.J.; EMBO J. 21, 2068-2075 (2002)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
MET8 gene
Saccharomyces cerevisiae
Crystallization (Commentary)
Crystallization
Organism
X-ray crystal structure of Met8p, hanging drop method
Saccharomyces cerevisiae
Engineering
Amino acid exchange
Commentary
Organism
D141A
mutant of bifunctional Met8p is completely inactive as both dehydrogenase and ferrochelatase
Saccharomyces cerevisiae
G22D
mutant of bifunctional Met8p is completely inactive as dehydrogenase, but functions as ferrochelatase
Saccharomyces cerevisiae
H237A
mutant of bifunctional Met8p is active as both dehydrogenase and ferrochelatase
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
sirohydrochlorin + Fe2+
Saccharomyces cerevisiae
-
siroheme + H+
-
-
?
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+
-
Saccharomyces cerevisiae
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
P15807
-
-
Saccharomyces cerevisiae
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant Met8p
Saccharomyces cerevisiae
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Saccharomyces cerevisiae
0.0311
-
wild-type Met8p
Saccharomyces cerevisiae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
sirohydrochlorin + Co2+
-
644283
Saccharomyces cerevisiae
cobalt-sirohydrochlorin + 2 H+
-
644283
Saccharomyces cerevisiae
?
sirohydrochlorin + Fe2+
-
644283
Saccharomyces cerevisiae
siroheme + H+
-
-
-
?
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
644283
Saccharomyces cerevisiae
siroheme + 2 H+
-
644283
Saccharomyces cerevisiae
?
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
644283
Saccharomyces cerevisiae
siroheme + 2 H+
-
644283
Saccharomyces cerevisiae
?
Subunits
Subunits
Commentary
Organism
homodimer
three structural domains per monomer, domain structure
Saccharomyces cerevisiae
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Saccharomyces cerevisiae
Cloned(Commentary) (protein specific)
Commentary
Organism
MET8 gene
Saccharomyces cerevisiae
Crystallization (Commentary) (protein specific)
Crystallization
Organism
X-ray crystal structure of Met8p, hanging drop method
Saccharomyces cerevisiae
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D141A
mutant of bifunctional Met8p is completely inactive as both dehydrogenase and ferrochelatase
Saccharomyces cerevisiae
G22D
mutant of bifunctional Met8p is completely inactive as dehydrogenase, but functions as ferrochelatase
Saccharomyces cerevisiae
H237A
mutant of bifunctional Met8p is active as both dehydrogenase and ferrochelatase
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
sirohydrochlorin + Fe2+
Saccharomyces cerevisiae
-
siroheme + H+
-
-
?
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+
-
Saccharomyces cerevisiae
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant Met8p
Saccharomyces cerevisiae
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Saccharomyces cerevisiae
0.0311
-
wild-type Met8p
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
sirohydrochlorin + Co2+
-
644283
Saccharomyces cerevisiae
cobalt-sirohydrochlorin + 2 H+
-
644283
Saccharomyces cerevisiae
?
sirohydrochlorin + Fe2+
-
644283
Saccharomyces cerevisiae
siroheme + H+
-
-
-
?
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
644283
Saccharomyces cerevisiae
siroheme + 2 H+
-
644283
Saccharomyces cerevisiae
?
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
644283
Saccharomyces cerevisiae
siroheme + 2 H+
-
644283
Saccharomyces cerevisiae
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
three structural domains per monomer, domain structure
Saccharomyces cerevisiae
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Saccharomyces cerevisiae
Other publictions for EC 4.99.1.4
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
748869
Garai
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1
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3
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1
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1
-
-
730419
Bali
Identification and characteriz ...
Paracoccus pantotrophus
Mol. Microbiol.
92
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-
1
1
-
-
-
-
-
-
1
1
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1
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1
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1
1
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1
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1
1
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729160
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Biochem. J.
444
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5
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1
1
2
1
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5
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1
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1
6
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1
1
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1
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1
1
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5
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1
1
2
1
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1
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1
6
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1
1
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716791
Romao
Evolution in a family of chela ...
Bacillus megaterium
Proc. Natl. Acad. Sci. USA
108
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2011
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1
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1
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1
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1
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696120
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no activity in Desulfovibrio vulgaris
Biochem. J.
420
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2009
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1
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665692
Raux-Deery
Identification and characteriz ...
Arabidopsis thaliana
J. Biol. Chem.
280
4713-4721
2005
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1
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2
1
1
2
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1
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4
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1
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2
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3
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1
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1
1
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1
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1
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2
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3
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649745
Raux
Identification and functional ...
Bacillus megaterium, Bacillus megaterium DSM 509
Biochem. J.
370
505-516
2003
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1
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1
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1
2
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4
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1
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2
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8
1
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1
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1
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1
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2
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8
1
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1
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653297
Stroupe
CysG structure reveals tetrapy ...
Salmonella enterica
Nat. Struct. Biol.
10
1064-1073
2003
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1
1
2
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1
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1
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1
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3
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1
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2
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1
1
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3
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3
1
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644283
Schubert
The structure of Saccharomyces ...
Saccharomyces cerevisiae
EMBO J.
21
2068-2075
2002
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1
1
3
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2
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2
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1
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4
1
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3
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1
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4
1
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1
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649817
Schubert
Structural diversity in metal ...
Saccharomyces cerevisiae
Biochem. Soc. Trans.
30
595-600
2002
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-
1
2
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1
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1
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1
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2
1
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1
2
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1
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