BRENDA - Enzyme Database
show all sequences of 1.8.1.2

Isolation of sulfite reductase variants of a commercial wine yeast with significantly reduced hydrogen sulfide production

Cordente, A.G.; Heinrich, A.; Pretorius, I.S.; Swiegers, J.H.; FEMS Yeast Res. 9, 446-459 (2009)

Data extracted from this reference:

Application
Application
Commentary
Organism
brewing
mutations in the sulfite reductase genes, MET5 and MET10, are responsible for low H2S phenotypes, yeast strains with reduced H2S production offer promising solutions to H2S-related taints generated during wine production
Saccharomyces cerevisiae
Cloned(Commentary)
Commentary
Organism
the MET5 and Met10 coding sequences are cloned into the vector pGEM-T-easy and subsequently into the centromeric Saccharomyces cerevisiae expression plasmid pRS416
Saccharomyces cerevisiae
Engineering
Amino acid exchange
Commentary
Organism
A979T
Met5p mutant
Saccharomyces cerevisiae
E1356K
Met5p mutant
Saccharomyces cerevisiae
E929K
Met10p mutant
Saccharomyces cerevisiae
G1115D
Met5p mutant
Saccharomyces cerevisiae
L606F
Met10p mutant
Saccharomyces cerevisiae
T990I
Met10p mutant
Saccharomyces cerevisiae
T997I
Met10p mutant
Saccharomyces cerevisiae
W59X
Met10p mutant
Saccharomyces cerevisiae
W841X
Met10p mutant
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
hydrogen sulfide + NADP+ + H2O
Saccharomyces cerevisiae
-
sulfite + NADPH + H+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
-
allele 1, subunit beta, MET5, subunit alpha, MET10; allele 2, subunit beta, MET5, subunit alpha, MET10
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
hydrogen sulfide + NADP+ + H2O
-
698012
Saccharomyces cerevisiae
sulfite + NADPH + H+
-
-
-
?
Subunits
Subunits
Commentary
Organism
heterotetramer
two alpha- and two beta-subunits, encoded by the MET10 and MET5 gene, respectively
Saccharomyces cerevisiae
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
-
Saccharomyces cerevisiae
FMN
-
Saccharomyces cerevisiae
iron-sulfur centre
-
Saccharomyces cerevisiae
NADPH
-
Saccharomyces cerevisiae
siroheme
-
Saccharomyces cerevisiae
Application (protein specific)
Application
Commentary
Organism
brewing
mutations in the sulfite reductase genes, MET5 and MET10, are responsible for low H2S phenotypes, yeast strains with reduced H2S production offer promising solutions to H2S-related taints generated during wine production
Saccharomyces cerevisiae
Cloned(Commentary) (protein specific)
Commentary
Organism
the MET5 and Met10 coding sequences are cloned into the vector pGEM-T-easy and subsequently into the centromeric Saccharomyces cerevisiae expression plasmid pRS416
Saccharomyces cerevisiae
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
-
Saccharomyces cerevisiae
FMN
-
Saccharomyces cerevisiae
iron-sulfur centre
-
Saccharomyces cerevisiae
NADPH
-
Saccharomyces cerevisiae
siroheme
-
Saccharomyces cerevisiae
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
A979T
Met5p mutant
Saccharomyces cerevisiae
E1356K
Met5p mutant
Saccharomyces cerevisiae
E929K
Met10p mutant
Saccharomyces cerevisiae
G1115D
Met5p mutant
Saccharomyces cerevisiae
L606F
Met10p mutant
Saccharomyces cerevisiae
T990I
Met10p mutant
Saccharomyces cerevisiae
T997I
Met10p mutant
Saccharomyces cerevisiae
W59X
Met10p mutant
Saccharomyces cerevisiae
W841X
Met10p mutant
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
hydrogen sulfide + NADP+ + H2O
Saccharomyces cerevisiae
-
sulfite + NADPH + H+
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
hydrogen sulfide + NADP+ + H2O
-
698012
Saccharomyces cerevisiae
sulfite + NADPH + H+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
heterotetramer
two alpha- and two beta-subunits, encoded by the MET10 and MET5 gene, respectively
Saccharomyces cerevisiae
Other publictions for EC 1.8.1.2
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)
742877
Askenasy
The N-terminal domain of Esch ...
Escherichia coli
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698012
Cordente
Isolation of sulfite reductase ...
Saccharomyces cerevisiae
FEMS Yeast Res.
9
446-459
2009
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Miller
Furfural inhibits growth by li ...
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696893
Zeng
Expression, purification and c ...
Acidithiobacillus ferrooxidans
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1239-1244
2008
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674504
Johnson
A new type of sulfite reductas ...
Methanocaldococcus jannaschii
J. Biol. Chem.
280
38776-38786
2005
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656421
Yin
-
Purification and characterizat ...
Escherichia coli
J. Food Sci.
67
3329-3334
2002
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1
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16
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392983
Willson
Cloning and characterization o ...
Actinobacillus pleuropneumoniae
Can. J. Vet. Res.
65
206-212
2001
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1
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6
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392987
Sohn
Ultradian metabolic oscillatio ...
Saccharomyces cerevisiae
Yeast
18
125-135
2001
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392986
Gruez
Four Crystal Structures of the ...
Escherichia coli
J. Mol. Biol.
299
199-212
2000
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392981
Coves
Overexpression of the FAD-bind ...
Escherichia coli
Biochem. J.
342
465-472
1999
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392988
Gruez
The FNR-like domain of the Esc ...
Escherichia coli
Acta Crystallogr. Sect. D
54
135-136
1998
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392980
Coves
Flavin mononucleotide-binding ...
Escherichia coli
Biochemistry
36
5921-5928
1997
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392985
Eschenbrenner
NADPH-sulfite reductase flavop ...
Escherichia coli
FEBS Lett.
374
82-84
1995
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392984
Gaudu
The NADPH:sulfite reductase of ...
Escherichia coli
Eur. J. Biochem.
226
459-463
1994
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392193
Coves
NADPH-Sulfite reductase from E ...
Escherichia coli
J. Biol. Chem.
268
18604-18609
1993
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392979
Arendsen
The dissimilatory sulfite redu ...
Desulfosarcina variabilis
Biochemistry
32
10323-10330
1993
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392975
Tei
Molecular cloning of the cys g ...
Escherichia coli
Biotechnol. Appl. Biochem.
12
212-216
1990
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392952
Ostrowski
Characterization of the flavop ...
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
J. Biol. Chem.
264
15796-15808
1989
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392953
Young
Activated conformers of Escher ...
Escherichia coli
Biochemistry
27
4991-4999
1988
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392976
Li
Cloning of the 3-phosphoadenyl ...
Escherichia coli
Gene
53
227-234
1987
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392954
McRee
The heme and Fe4S4 cluster in ...
Escherichia coli
J. Biol. Chem.
261
10277-10281
1986
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392955
Kobayashi
Studies on yeast sulfite reduc ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
709
38-45
1982
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392956
Kobayashi
Studies on yeast sulfite reduc ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
709
46-52
1982
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392957
Kobayashi
Studies on yeast sulfite reduc ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
705
348-356
1982
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392958
Siegel
Escherichia coli sulfite reduc ...
Escherichia coli
J. Biol. Chem.
257
6343-6350
1982
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2
3
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392977
McRee
Preliminary X-ray diffraction ...
Escherichia coli
J. Mol. Biol.
154
179-180
1982
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392978
Scott
-
Sirohydrochlorin. Prosthetic g ...
Propionibacterium freudenreichii subsp. shermanii
J. Am. Chem. Soc.
100
7987-7994
1978
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287801
Hatefi
-
Metal-containing flavoprotein ...
Escherichia coli, Neurospora crassa, Saccharomyces cerevisiae, Salmonella enterica subsp. enterica serovar Typhimurium
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
13
175-297
1976
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14
2
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20
2
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392960
Dott
-
Sulfite formation by wine yeas ...
Saccharomyces bayanus, Saccharomyces cerevisiae
Arch. Microbiol.
108
99-104
1976
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4
2
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392961
Murphy
Reduced nicotinamide adenine d ...
Escherichia coli
J. Biol. Chem.
249
1610-1614
1974
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392962
Siegel
Reduced nicotinamide adenine d ...
Escherichia coli
J. Biol. Chem.
249
1587-1598
1974
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392963
Faeder
Reduced nicotinamide adenine d ...
Escherichia coli
J. Biol. Chem.
249
1599-1609
1974
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392964
Siegel
Reduced nicotinamide adenine d ...
Escherichia coli
J. Biol. Chem.
249
1572-1586
1974
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11
3
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7
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3
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11
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7
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12
3
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392965
Murphy
Siroheme and sirohydrochlorin. ...
Desulfotomaculum nigrificans
J. Biol. Chem.
248
6911-6919
1973
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392966
Murphy
Reduced nicotinamide adenine d ...
Escherichia coli
J. Biol. Chem.
248
2801-2814
1973
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392967
Siegel
Reduced nicotinamide adenine d ...
Escherichia coli
J. Biol. Chem.
248
251-264
1973
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392968
Siegel
-
TPNH-Sulfite reductase (Escher ...
Escherichia coli
Methods Enzymol.
17B
539-545
1971
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5
2
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4
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392969
Yoshimoto
-
Sulfite reductase (bakers¦ ye ...
Saccharomyces cerevisiae
Methods Enzymol.
17B
520-528
1971
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5
6
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6
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392970
Hoeksema
Characterization of a thermola ...
Salmonella enterica subsp. enterica serovar Pullorum
J. Bacteriol.
108
154-158
1971
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392974
Yoshimoto
Studies on yeast sulfite reduc ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
220
190-205
1970
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392973
Prabhakararao
Sulphite reductase from bakers ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
180
253-263
1969
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6
4
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392971
Yoshimoto
Studies on yeast sulfite reduc ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
153
555-575
1968
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5
3
1
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5
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5
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392972
Yoshimoto
Studies on yeast sulfite reduc ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
153
576-588
1968
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