BRENDA - Enzyme Database
show all sequences of 2.5.1.73

RNA-dependent cysteine biosynthesis in archea

Sauerwald, A.; Zhu, W.; Major, T.A.; Roy, H.; Palioura, S.; Jahn, D.; Whitman, W.B.; Yates, J.R.; Ibba, M.; Soell, D.; Science 307, 1969-1972 (2005)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene Mj1678 or pscS, functional complementation of a cysteinyl-tRNACys synthase mutant strain, phylogenetic analysis, expression in Escherichia coli
Methanocaldococcus jannaschii
Engineering
Amino acid exchange
Commentary
Organism
additional information
the enzyme can synthesize Cys-tRNACys in a sepS deletion mutant when Na2S and O-phosphoserine are exogenously added, sepS encodes the O-phosphoseryl-tRNA synthetase, EC 6.1.1.B2
Methanococcus maripaludis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
O-phospho-L-seryl-tRNACys + sulfide
Methanococcus maripaludis
the natural sulfur donor is not characterized, the activity of SepCysS provides a means by which both cysteine and selenocysteine can be added to the genetic code, the enzyme is responsible for Cys-tRNACys synthesis together with the O-phosphoseryl-tRNA synthetase in the organism containing a dispensable cysteinyl-tRNACys synthase, EC 6.1.1.16, overview
L-cysteinyl-tRNACys + phosphate
-
-
-
O-phospho-L-seryl-tRNACys + sulfide
Methanocaldococcus jannaschii
the natural sulfur donor is not characterized, the activity of SepCysS provides a means by which both cysteine and selenocysteine can be added to the genetic code, the enzyme is responsible for Cys-tRNACys synthesis together with the O-phosphoseryl-tRNA synthetase in the organism lacking the cysteinyl-tRNACys synthase, EC 6.1.1.16, overview
L-cysteinyl-tRNACys + phosphate
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanocaldococcus jannaschii
-
gene Mj1678 or pscS
-
Methanococcus maripaludis
A4FWT8
gene pcsS
-
Purification (Commentary)
Commentary
Organism
native enzyme to homogeneity
Methanocaldococcus jannaschii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
O-phospho-L-seryl-tRNACys + sulfide
the natural sulfur donor is not characterized, the activity of SepCysS provides a means by which both cysteine and selenocysteine can be added to the genetic code, the enzyme is responsible for Cys-tRNACys synthesis together with the O-phosphoseryl-tRNA synthetase in the organism containing a dispensable cysteinyl-tRNACys synthase, EC 6.1.1.16, overview
677118
Methanococcus maripaludis
L-cysteinyl-tRNACys + phosphate
-
-
-
-
O-phospho-L-seryl-tRNACys + sulfide
the natural sulfur donor is not characterized, the activity of SepCysS provides a means by which both cysteine and selenocysteine can be added to the genetic code, the enzyme is responsible for Cys-tRNACys synthesis together with the O-phosphoseryl-tRNA synthetase in the organism lacking the cysteinyl-tRNACys synthase, EC 6.1.1.16, overview
677118
Methanocaldococcus jannaschii
L-cysteinyl-tRNACys + phosphate
-
-
-
-
O-phospho-L-seryl-tRNACys + sulfide
sulfide e.g. from Na2S, anaerobic reaction
677118
Methanocaldococcus jannaschii
L-cysteinyl-tRNACys + phosphate
-
-
-
-
O-phospho-L-seryl-tRNACys + sulfide
sulfide e.g. from Na2S, anaerobic reaction
677118
Methanococcus maripaludis
L-cysteinyl-tRNACys + phosphate
-
-
-
-
Cofactor
Cofactor
Commentary
Organism
Structure
pyridoxal 5'-phosphate
-
Methanocaldococcus jannaschii
pyridoxal 5'-phosphate
-
Methanococcus maripaludis
Cloned(Commentary) (protein specific)
Commentary
Organism
gene Mj1678 or pscS, functional complementation of a cysteinyl-tRNACys synthase mutant strain, phylogenetic analysis, expression in Escherichia coli
Methanocaldococcus jannaschii
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
pyridoxal 5'-phosphate
-
Methanocaldococcus jannaschii
pyridoxal 5'-phosphate
-
Methanococcus maripaludis
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
the enzyme can synthesize Cys-tRNACys in a sepS deletion mutant when Na2S and O-phosphoserine are exogenously added, sepS encodes the O-phosphoseryl-tRNA synthetase, EC 6.1.1.B2
Methanococcus maripaludis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
O-phospho-L-seryl-tRNACys + sulfide
Methanococcus maripaludis
the natural sulfur donor is not characterized, the activity of SepCysS provides a means by which both cysteine and selenocysteine can be added to the genetic code, the enzyme is responsible for Cys-tRNACys synthesis together with the O-phosphoseryl-tRNA synthetase in the organism containing a dispensable cysteinyl-tRNACys synthase, EC 6.1.1.16, overview
L-cysteinyl-tRNACys + phosphate
-
-
-
O-phospho-L-seryl-tRNACys + sulfide
Methanocaldococcus jannaschii
the natural sulfur donor is not characterized, the activity of SepCysS provides a means by which both cysteine and selenocysteine can be added to the genetic code, the enzyme is responsible for Cys-tRNACys synthesis together with the O-phosphoseryl-tRNA synthetase in the organism lacking the cysteinyl-tRNACys synthase, EC 6.1.1.16, overview
L-cysteinyl-tRNACys + phosphate
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
native enzyme to homogeneity
Methanocaldococcus jannaschii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
O-phospho-L-seryl-tRNACys + sulfide
the natural sulfur donor is not characterized, the activity of SepCysS provides a means by which both cysteine and selenocysteine can be added to the genetic code, the enzyme is responsible for Cys-tRNACys synthesis together with the O-phosphoseryl-tRNA synthetase in the organism containing a dispensable cysteinyl-tRNACys synthase, EC 6.1.1.16, overview
677118
Methanococcus maripaludis
L-cysteinyl-tRNACys + phosphate
-
-
-
-
O-phospho-L-seryl-tRNACys + sulfide
the natural sulfur donor is not characterized, the activity of SepCysS provides a means by which both cysteine and selenocysteine can be added to the genetic code, the enzyme is responsible for Cys-tRNACys synthesis together with the O-phosphoseryl-tRNA synthetase in the organism lacking the cysteinyl-tRNACys synthase, EC 6.1.1.16, overview
677118
Methanocaldococcus jannaschii
L-cysteinyl-tRNACys + phosphate
-
-
-
-
O-phospho-L-seryl-tRNACys + sulfide
sulfide e.g. from Na2S, anaerobic reaction
677118
Methanocaldococcus jannaschii
L-cysteinyl-tRNACys + phosphate
-
-
-
-
O-phospho-L-seryl-tRNACys + sulfide
sulfide e.g. from Na2S, anaerobic reaction
677118
Methanococcus maripaludis
L-cysteinyl-tRNACys + phosphate
-
-
-
-
Other publictions for EC 2.5.1.73
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)
728697
Liu
Ancient translation factor is ...
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661
Proc. Natl. Acad. Sci. USA
111
10520-10505
2014
1
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1
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5
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722286
Helgadottir
Mutational analysis of Sep-tRN ...
Methanocaldococcus jannaschii
FEBS Lett.
586
60-63
2012
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19
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3
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19
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722799
Liu
Catalytic mechanism of Sep-tRN ...
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661
J. Biol. Chem.
287
5426-5433
2012
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1
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6
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6
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1
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4
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1
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6
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1
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4
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1
1
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722261
Yuan
A tRNA-dependent cysteine bios ...
Escherichia coli
FEBS Lett.
584
2857-2861
2010
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2
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2
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2
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684126
Yuan
Amino acid modifications on tR ...
Archaeoglobus fulgidus, Methanococcus maripaludis, no activity in Methanobrevibacter smithii, no activity in Methanosphaera stadtmanae
Acta Biochim. Biophys. Sin. (Shanghai)
40
539-553
2008
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1
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1
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5
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4
1
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2
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2
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4
1
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687743
Hauenstein
Redundant synthesis of cystein ...
Methanosarcina mazei
J. Biol. Chem.
283
22007-22017
2008
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1
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3
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4
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1
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1
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3
1
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1
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2
2
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3
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2
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1
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3
1
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689145
Zhang
Aminoacylation of tRNA with ph ...
Methanocaldococcus jannaschii
Nat. Struct. Mol. Biol.
15
507-514
2008
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1
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1
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3
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1
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3
1
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1
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1
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1
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3
1
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675447
Fukunaga
Structural insights into the s ...
Archaeoglobus fulgidus
J. Mol. Biol.
370
128-141
2007
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1
1
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1
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2
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3
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1
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4
2
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1
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1
1
1
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1
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2
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1
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4
2
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676784
O'Donoghue
The evolutionary history of Cy ...
Archaeoglobus fulgidus, Methanococcoides burtonii, Methanopyrus kandleri, Methanospirillum hungatei
Proc. Natl. Acad. Sci. USA
102
19003-19008
2005
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4
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4
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4
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8
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4
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4
4
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4
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8
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677118
Sauerwald
RNA-dependent cysteine biosynt ...
Methanocaldococcus jannaschii, Methanococcus maripaludis
Science
307
1969-1972
2005
-
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1
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1
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2
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5
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1
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4
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2
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1
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1
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4
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