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show all sequences of 1.14.99.51

Genetic and metabolomic dissection of the ergothioneine and selenoneine biosynthetic pathway in the fission yeast, S. pombe, and construction of an overproduction system

Pluskal, T.; Ueno, M.; Yanagida, M.; PLoS ONE 9, e97774 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene egt1+, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic tree
Schizosaccharomyces pombe
Engineering
Amino acid exchange
Commentary
Organism
additional information
construction of an egt1+ overexpression system by replacing its native promoter with the nmt1+ promoter, which is inducible in the absence of thiamine. Generation of a egt1+ deletion mutant, DELTAegt1, by replacing the target loci in the wild-type 972 strain with the kanamycin resistance marker (kanMX) leading to absence of all ergothioneine pathway intermediates and ergothioneine itself in DELTAegt1. Employment of three versions of the nmt1 promoter plasmid with increasing strength of expression and constructed three strains P81nmt1-egt1+, P41nmt1-egt1+, and P3nmt1-egt1+, respectively. Mutant DELTAegt1 strain shows no growth defects during cultivation in either rich (YE) or minimal (EMM2) culture media, deletion of gene egt1+ causes no significant perturbation to the intracellular metabolome of quiescent cells. No sensitivity or resistance of the mutant strains to oxidative stress compared to wild-type 972 strain
Schizosaccharomyces pombe
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
required for catalysis
Schizosaccharomyces pombe
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
hercynine + L-cysteine + O2
Schizosaccharomyces pombe
-
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
?
hercynine + L-cysteine + O2
Schizosaccharomyces pombe 972
-
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
?
additional information
Schizosaccharomyces pombe
the ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium. Selenoneine biosynthesis, unlike ergothioneine biosynthesis, does not produce a sulfoxide as its intermediate, but produces hercynylselenocysteine instead. Enzyme Egt-1 also catalyzes the synthesis of hercynine, EC 2.1.1.44
?
-
-
-
additional information
Schizosaccharomyces pombe 972
the ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium. Selenoneine biosynthesis, unlike ergothioneine biosynthesis, does not produce a sulfoxide as its intermediate, but produces hercynylselenocysteine instead. Enzyme Egt-1 also catalyzes the synthesis of hercynine, EC 2.1.1.44
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Schizosaccharomyces pombe
O94632
-
-
Schizosaccharomyces pombe 972
O94632
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
hercynine + L-cysteine + O2
-
743662
Schizosaccharomyces pombe
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
hercynine + L-cysteine + O2
-
743662
Schizosaccharomyces pombe 972
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
additional information
the ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium. Selenoneine biosynthesis, unlike ergothioneine biosynthesis, does not produce a sulfoxide as its intermediate, but produces hercynylselenocysteine instead. Enzyme Egt-1 also catalyzes the synthesis of hercynine, EC 2.1.1.44
743662
Schizosaccharomyces pombe
?
-
-
-
-
additional information
hercynylcysteine sulfoxide can spontaneously convert into ergothioneine in the presence of pyridoxal 5'-phosphate
743662
Schizosaccharomyces pombe
?
-
-
-
-
additional information
the ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium. Selenoneine biosynthesis, unlike ergothioneine biosynthesis, does not produce a sulfoxide as its intermediate, but produces hercynylselenocysteine instead. Enzyme Egt-1 also catalyzes the synthesis of hercynine, EC 2.1.1.44
743662
Schizosaccharomyces pombe 972
?
-
-
-
-
additional information
hercynylcysteine sulfoxide can spontaneously convert into ergothioneine in the presence of pyridoxal 5'-phosphate
743662
Schizosaccharomyces pombe 972
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
More
Egt-1 domain structure, overview
Schizosaccharomyces pombe
Cloned(Commentary) (protein specific)
Commentary
Organism
gene egt1+, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic tree
Schizosaccharomyces pombe
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
construction of an egt1+ overexpression system by replacing its native promoter with the nmt1+ promoter, which is inducible in the absence of thiamine. Generation of a egt1+ deletion mutant, DELTAegt1, by replacing the target loci in the wild-type 972 strain with the kanamycin resistance marker (kanMX) leading to absence of all ergothioneine pathway intermediates and ergothioneine itself in DELTAegt1. Employment of three versions of the nmt1 promoter plasmid with increasing strength of expression and constructed three strains P81nmt1-egt1+, P41nmt1-egt1+, and P3nmt1-egt1+, respectively. Mutant DELTAegt1 strain shows no growth defects during cultivation in either rich (YE) or minimal (EMM2) culture media, deletion of gene egt1+ causes no significant perturbation to the intracellular metabolome of quiescent cells. No sensitivity or resistance of the mutant strains to oxidative stress compared to wild-type 972 strain
Schizosaccharomyces pombe
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
required for catalysis
Schizosaccharomyces pombe
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
hercynine + L-cysteine + O2
Schizosaccharomyces pombe
-
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
?
hercynine + L-cysteine + O2
Schizosaccharomyces pombe 972
-
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
?
additional information
Schizosaccharomyces pombe
the ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium. Selenoneine biosynthesis, unlike ergothioneine biosynthesis, does not produce a sulfoxide as its intermediate, but produces hercynylselenocysteine instead. Enzyme Egt-1 also catalyzes the synthesis of hercynine, EC 2.1.1.44
?
-
-
-
additional information
Schizosaccharomyces pombe 972
the ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium. Selenoneine biosynthesis, unlike ergothioneine biosynthesis, does not produce a sulfoxide as its intermediate, but produces hercynylselenocysteine instead. Enzyme Egt-1 also catalyzes the synthesis of hercynine, EC 2.1.1.44
?
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
hercynine + L-cysteine + O2
-
743662
Schizosaccharomyces pombe
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
hercynine + L-cysteine + O2
-
743662
Schizosaccharomyces pombe 972
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
additional information
the ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium. Selenoneine biosynthesis, unlike ergothioneine biosynthesis, does not produce a sulfoxide as its intermediate, but produces hercynylselenocysteine instead. Enzyme Egt-1 also catalyzes the synthesis of hercynine, EC 2.1.1.44
743662
Schizosaccharomyces pombe
?
-
-
-
-
additional information
hercynylcysteine sulfoxide can spontaneously convert into ergothioneine in the presence of pyridoxal 5'-phosphate
743662
Schizosaccharomyces pombe
?
-
-
-
-
additional information
the ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium. Selenoneine biosynthesis, unlike ergothioneine biosynthesis, does not produce a sulfoxide as its intermediate, but produces hercynylselenocysteine instead. Enzyme Egt-1 also catalyzes the synthesis of hercynine, EC 2.1.1.44
743662
Schizosaccharomyces pombe 972
?
-
-
-
-
additional information
hercynylcysteine sulfoxide can spontaneously convert into ergothioneine in the presence of pyridoxal 5'-phosphate
743662
Schizosaccharomyces pombe 972
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
More
Egt-1 domain structure, overview
Schizosaccharomyces pombe
General Information
General Information
Commentary
Organism
evolution
mug158+/SPBC1604.01 is a distant homologue of the mycobacterial EgtD and EgtB genes, encoding a single fusion protein. The Schizosaccharomyces pombe homologue utilizes cysteine as a substrate, rather than using gamma-glutamyl-cysteine, as in the case of the bacterial EgtB enzyme, EC 1.14.99.50
Schizosaccharomyces pombe
metabolism
the enzyme produces hercynylcysteine sulfoxide in the ergothioneine pathway. The ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium. Selenoneine biosynthesis involves an intermediate compound, hercynylselenocysteine
Schizosaccharomyces pombe
physiological function
contribution of gene egt1+ to oxidative stress response, but gene egt1+ might not be among the primary mechanisms that protect Schizosaccharomyces pombe from exogenous peroxide
Schizosaccharomyces pombe
General Information (protein specific)
General Information
Commentary
Organism
evolution
mug158+/SPBC1604.01 is a distant homologue of the mycobacterial EgtD and EgtB genes, encoding a single fusion protein. The Schizosaccharomyces pombe homologue utilizes cysteine as a substrate, rather than using gamma-glutamyl-cysteine, as in the case of the bacterial EgtB enzyme, EC 1.14.99.50
Schizosaccharomyces pombe
metabolism
the enzyme produces hercynylcysteine sulfoxide in the ergothioneine pathway. The ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium. Selenoneine biosynthesis involves an intermediate compound, hercynylselenocysteine
Schizosaccharomyces pombe
physiological function
contribution of gene egt1+ to oxidative stress response, but gene egt1+ might not be among the primary mechanisms that protect Schizosaccharomyces pombe from exogenous peroxide
Schizosaccharomyces pombe
Other publictions for EC 1.14.99.51
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)
732793
Pluskal
Genetic and metabolomic dissec ...
Schizosaccharomyces pombe
PLoS One
9
e97774
2014
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1
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1
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7
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3
1
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1
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1
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3
1
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1
1
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734829
Hu
Bioinformatic and biochemical ...
Neurospora crassa, Neurospora crassa ATCC 24698
Org. Lett.
16
5382-5385
2014
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1
1
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4
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1
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2
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4
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6
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2
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1
1
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4
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1
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2
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6
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2
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1
1
-
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743388
Hu
Bioinformatic and biochemical ...
Neurospora crassa, Neurospora crassa ATCC 24698
Org. Lett.
16
5382-5385
2014
-
1
1
-
-
-
-
4
-
1
-
4
-
4
-
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6
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4
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1
1
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4
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1
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4
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6
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4
-
-
-
-
-
2
2
-
-
-
743662
Pluskal
Genetic and metabolomic disse ...
Schizosaccharomyces pombe, Schizosaccharomyces pombe 972
PLoS ONE
9
e97774
2014
-
-
1
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1
-
-
-
-
1
-
4
-
8
-
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6
1
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1
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1
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1
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4
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-
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6
1
-
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-
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3
3
-
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733921
Bello
The Neurospora crassa mutant N ...
Neurospora crassa, Neurospora crassa ATCC 24698, no activity in Bremia lactucae, no activity in Candida albicans, no activity in Pichia ssp., no activity in Saccharomyces cerevisiae
Fungal Genet. Biol.
49
160-172
2012
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1
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8
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2
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2
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2
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4
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