BRENDA - Enzyme Database
show all sequences of 2.5.1.73

Catalytic mechanism of Sep-tRNA:Cys-tRNA synthase: sulfur transfer is mediated by disulfide and persulfide

Liu, Y.; Dos Santos, P.C.; Zhu, X.; Orlando, R.; Dean, D.R.; Soell, D.; Yuan, J.; J. Biol. Chem. 287, 5426-5433 (2012)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherchia coli
Methanocaldococcus jannaschii
Engineering
Amino acid exchange
Commentary
Organism
C113A
activity similar to wild-type
Methanocaldococcus jannaschii
C209A
activity similar to wild-type
Methanocaldococcus jannaschii
C272A
loss of the ability to complement an Escherichia coli selA knockout strain, which cannot produce active formate dehydrogenase H due to the lack of selenocysteine incorporation
Methanocaldococcus jannaschii
C64A
loss of the ability to complement an Escherichia coli selA knockout strain, which cannot produce active formate dehydrogenase H due to the lack of selenocysteine incorporation
Methanocaldococcus jannaschii
C67A
loss of the ability to complement an Escherichia coli selA knockout strain, which cannot produce active formate dehydrogenase H due to the lack of selenocysteine incorporation
Methanocaldococcus jannaschii
K234A
complete loss of activtiy
Methanocaldococcus jannaschii
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanocaldococcus jannaschii
Q59072
-
-
Methanocaldococcus jannaschii DSM 2661
Q59072
-
-
Purification (Commentary)
Commentary
Organism
-
Methanocaldococcus jannaschii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the highly conserved Cys residues Cys64, Cys67, and Cys272 are essential for the sulfhydrylation reaction in vivo. Cys64 and Cys67 form a disulfide linkage and carry a sulfane sulfur in a portion of the enzyme, suggesting that a persulfide group containing a sulfane sulfur is the proximal sulfur donor for cysteine biosynthesis. The presence of Cys272 increases the amount of sulfane sulfur in the enzyme by 3fold, suggesting that this Cys residue facilitates the generation of the persulfide group. A sulfur relay mechanism recruits both disulfide and persulfide intermediates
722799
Methanocaldococcus jannaschii
?
-
-
-
-
additional information
the highly conserved Cys residues Cys64, Cys67, and Cys272 are essential for the sulfhydrylation reaction in vivo. Cys64 and Cys67 form a disulfide linkage and carry a sulfane sulfur in a portion of the enzyme, suggesting that a persulfide group containing a sulfane sulfur is the proximal sulfur donor for cysteine biosynthesis. The presence of Cys272 increases the amount of sulfane sulfur in the enzyme by 3fold, suggesting that this Cys residue facilitates the generation of the persulfide group. A sulfur relay mechanism recruits both disulfide and persulfide intermediates
722799
Methanocaldococcus jannaschii DSM 2661
?
-
-
-
-
O-phospho-L-seryl-tRNACys + sulfide
all three highly conserved Cys residues in the enzyme (Cys64, Cys67, and Cys272) are essential for the sulfhydrylation reaction in vivo. Cys64 and Cys67 form a disulfide linkage and carry a sulfane sulfur in a portion of the enzyme. A persulfide group (containing a sulfane sulfur) is the proximal sulfur donor for cysteine biosynthesis
722799
Methanocaldococcus jannaschii
L-cysteinyl-tRNACys + phosphate
-
-
-
?
O-phospho-L-seryl-tRNACys + sulfide
all three highly conserved Cys residues in the enzyme (Cys64, Cys67, and Cys272) are essential for the sulfhydrylation reaction in vivo. Cys64 and Cys67 form a disulfide linkage and carry a sulfane sulfur in a portion of the enzyme. A persulfide group (containing a sulfane sulfur) is the proximal sulfur donor for cysteine biosynthesis
722799
Methanocaldococcus jannaschii DSM 2661
L-cysteinyl-tRNACys + phosphate
-
-
-
?
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherchia coli
Methanocaldococcus jannaschii
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
C113A
activity similar to wild-type
Methanocaldococcus jannaschii
C209A
activity similar to wild-type
Methanocaldococcus jannaschii
C272A
loss of the ability to complement an Escherichia coli selA knockout strain, which cannot produce active formate dehydrogenase H due to the lack of selenocysteine incorporation
Methanocaldococcus jannaschii
C64A
loss of the ability to complement an Escherichia coli selA knockout strain, which cannot produce active formate dehydrogenase H due to the lack of selenocysteine incorporation
Methanocaldococcus jannaschii
C67A
loss of the ability to complement an Escherichia coli selA knockout strain, which cannot produce active formate dehydrogenase H due to the lack of selenocysteine incorporation
Methanocaldococcus jannaschii
K234A
complete loss of activtiy
Methanocaldococcus jannaschii
Purification (Commentary) (protein specific)
Commentary
Organism
-
Methanocaldococcus jannaschii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the highly conserved Cys residues Cys64, Cys67, and Cys272 are essential for the sulfhydrylation reaction in vivo. Cys64 and Cys67 form a disulfide linkage and carry a sulfane sulfur in a portion of the enzyme, suggesting that a persulfide group containing a sulfane sulfur is the proximal sulfur donor for cysteine biosynthesis. The presence of Cys272 increases the amount of sulfane sulfur in the enzyme by 3fold, suggesting that this Cys residue facilitates the generation of the persulfide group. A sulfur relay mechanism recruits both disulfide and persulfide intermediates
722799
Methanocaldococcus jannaschii
?
-
-
-
-
additional information
the highly conserved Cys residues Cys64, Cys67, and Cys272 are essential for the sulfhydrylation reaction in vivo. Cys64 and Cys67 form a disulfide linkage and carry a sulfane sulfur in a portion of the enzyme, suggesting that a persulfide group containing a sulfane sulfur is the proximal sulfur donor for cysteine biosynthesis. The presence of Cys272 increases the amount of sulfane sulfur in the enzyme by 3fold, suggesting that this Cys residue facilitates the generation of the persulfide group. A sulfur relay mechanism recruits both disulfide and persulfide intermediates
722799
Methanocaldococcus jannaschii DSM 2661
?
-
-
-
-
O-phospho-L-seryl-tRNACys + sulfide
all three highly conserved Cys residues in the enzyme (Cys64, Cys67, and Cys272) are essential for the sulfhydrylation reaction in vivo. Cys64 and Cys67 form a disulfide linkage and carry a sulfane sulfur in a portion of the enzyme. A persulfide group (containing a sulfane sulfur) is the proximal sulfur donor for cysteine biosynthesis
722799
Methanocaldococcus jannaschii
L-cysteinyl-tRNACys + phosphate
-
-
-
?
O-phospho-L-seryl-tRNACys + sulfide
all three highly conserved Cys residues in the enzyme (Cys64, Cys67, and Cys272) are essential for the sulfhydrylation reaction in vivo. Cys64 and Cys67 form a disulfide linkage and carry a sulfane sulfur in a portion of the enzyme. A persulfide group (containing a sulfane sulfur) is the proximal sulfur donor for cysteine biosynthesis
722799
Methanocaldococcus jannaschii DSM 2661
L-cysteinyl-tRNACys + phosphate
-
-
-
?
General Information
General Information
Commentary
Organism
physiological function
wild-type enzyme can complement an Escherichia coli selA knockout strain, which cannot produce active formate dehydrogenase H due to the lack of selenocysteine incorporation
Methanocaldococcus jannaschii
General Information (protein specific)
General Information
Commentary
Organism
physiological function
wild-type enzyme can complement an Escherichia coli selA knockout strain, which cannot produce active formate dehydrogenase H due to the lack of selenocysteine incorporation
Methanocaldococcus jannaschii
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
-
-
1
-
6
-
-
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-
-
-
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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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-
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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
-
-
-
1
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-
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1
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5
-
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-
-
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4
1
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2
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3
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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-
-
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3
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4
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1
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1
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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
-
-
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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-
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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
-
-
1
1
-
-
-
-
-
1
-
2
-
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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1
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