BRENDA - Enzyme Database show
show all sequences of 2.9.1.2

Structural insights into RNA-dependent eukaryal and archaeal selenocysteine formation

Araiso, Y.; Palioura, S.; Ishitani, R.; Sherrer, R.L.; O'Donoghue, P.; Yuan, J.; Oshikane, H.; Domae, N.; Defranco, J.; Söll, D.; Nureki, O.; Nucleic Acids Res. 36, 1187-1199 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Methanococcus maripaludis
Crystallization (Commentary)
Crystallization
Organism
sitting-drop vapor diffusion method at 20°C, crystal structure of the enzyme complexed with pyridoxal 5'-phosphate at 2.5 A resolution
Methanococcus maripaludis
Engineering
Amino acid exchange
Commentary
Organism
H166A
the mutant is partially active in forming Sec-tRNASec in vivo. In vitro, the mutant is partially active in forming Cys-tRNASec
Methanococcus maripaludis
H166F
mutant is inactive in vivo
Methanococcus maripaludis
H166Q
mutant is inactive in vivo
Methanococcus maripaludis
R307A
the mutant is significantly less active in L-selenocysteinyl-tRNASec formation in vivo and Cys-tRNASec formation in vitro
Methanococcus maripaludis
R72A
the mutant enzyme is significantly less active in L-selenocysteinyl-tRNASec formation in vivo and Cys-tRNASec formation in vitro. The mutant enzyme is unable to form L-selenocysteinyl-tRNASec in vitro
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-tRNASec + selenophosphate
Methanococcus maripaludis
the micronutrient selenium is present in proteins as selenocysteine. In eukaryotes and archaea, selenocysteine is formed in a tRNA-dependent conversion of O-phosphoserine by O-phosphoseryltRNA:selenocysteinyl-tRNA synthase
L-selenocysteinyl-tRNASec + phosphate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanococcus maripaludis
Q6LZM9
-
-
Purification (Commentary)
Commentary
Organism
recombinent enzyme
Methanococcus maripaludis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
O-phospho-L-seryl-tRNASec + selenophosphate
-
694428
Methanococcus maripaludis
L-selenocysteinyl-tRNASec + phosphate
-
-
-
?
O-phospho-L-seryl-tRNASec + selenophosphate
the micronutrient selenium is present in proteins as selenocysteine. In eukaryotes and archaea, selenocysteine is formed in a tRNA-dependent conversion of O-phosphoserine by O-phosphoseryltRNA:selenocysteinyl-tRNA synthase
694428
Methanococcus maripaludis
L-selenocysteinyl-tRNASec + phosphate
-
-
-
?
Subunits
Subunits
Commentary
Organism
tetramer
a member of the Fold Type I pyridoxal 5'-phosphate enzyme family, forms an (alpha2)2 homotetramer through its N-terminal extension. The active site lies on the dimer interface with each monomer contributing essential residues
Methanococcus maripaludis
Cofactor
Cofactor
Commentary
Organism
Structure
pyridoxal 5'-phosphate
pyridoxal 5'-phosphate is covalently bound to the conserved Lys278
Methanococcus maripaludis
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Methanococcus maripaludis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
pyridoxal 5'-phosphate
pyridoxal 5'-phosphate is covalently bound to the conserved Lys278
Methanococcus maripaludis
Crystallization (Commentary) (protein specific)
Crystallization
Organism
sitting-drop vapor diffusion method at 20°C, crystal structure of the enzyme complexed with pyridoxal 5'-phosphate at 2.5 A resolution
Methanococcus maripaludis
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
H166A
the mutant is partially active in forming Sec-tRNASec in vivo. In vitro, the mutant is partially active in forming Cys-tRNASec
Methanococcus maripaludis
H166F
mutant is inactive in vivo
Methanococcus maripaludis
H166Q
mutant is inactive in vivo
Methanococcus maripaludis
R307A
the mutant is significantly less active in L-selenocysteinyl-tRNASec formation in vivo and Cys-tRNASec formation in vitro
Methanococcus maripaludis
R72A
the mutant enzyme is significantly less active in L-selenocysteinyl-tRNASec formation in vivo and Cys-tRNASec formation in vitro. The mutant enzyme is unable to form L-selenocysteinyl-tRNASec in vitro
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-tRNASec + selenophosphate
Methanococcus maripaludis
the micronutrient selenium is present in proteins as selenocysteine. In eukaryotes and archaea, selenocysteine is formed in a tRNA-dependent conversion of O-phosphoserine by O-phosphoseryltRNA:selenocysteinyl-tRNA synthase
L-selenocysteinyl-tRNASec + phosphate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinent enzyme
Methanococcus maripaludis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
O-phospho-L-seryl-tRNASec + selenophosphate
-
694428
Methanococcus maripaludis
L-selenocysteinyl-tRNASec + phosphate
-
-
-
?
O-phospho-L-seryl-tRNASec + selenophosphate
the micronutrient selenium is present in proteins as selenocysteine. In eukaryotes and archaea, selenocysteine is formed in a tRNA-dependent conversion of O-phosphoserine by O-phosphoseryltRNA:selenocysteinyl-tRNA synthase
694428
Methanococcus maripaludis
L-selenocysteinyl-tRNASec + phosphate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
a member of the Fold Type I pyridoxal 5'-phosphate enzyme family, forms an (alpha2)2 homotetramer through its N-terminal extension. The active site lies on the dimer interface with each monomer contributing essential residues
Methanococcus maripaludis
Other publictions for EC 2.9.1.2
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)
738683
Manhas
Leishmania donovani encodes a ...
Leishmania donovani, Leishmania donovani Bob
J. Biol. Chem.
291
1203-1220
2016
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1
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2
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8
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1
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2
1
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1
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1
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2
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1
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2
1
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-
1
1
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739263
Zhao
The role of Sep (O-phosphoseri ...
Homo sapiens
Placenta
34
967-972
2013
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2
2
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723559
Li
Priority in selenium homeostas ...
Gallus gallus
PLoS ONE
7
e35761
2012
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1
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1
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723214
Hohn
Genetic analysis of selenocyst ...
Methanococcus maripaludis
Mol. Microbiol.
81
249-258
2011
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4
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1
1
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694074
Aeby
The selenoproteome is dispensa ...
Trypanosoma brucei
Mol. Biochem. Parasitol.
168
191-193
2009
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1
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2
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1
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694917
Aeby
The canonical pathway for sele ...
Trypanosoma brucei
Proc. Natl. Acad. Sci. USA
106
5088-5092
2009
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1
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6
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695136
Palioura
The human SepSecS-tRNASec comp ...
Homo sapiens
Science
325
321-325
2009
-
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1
7
-
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1
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2
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1
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2
1
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1
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1
1
7
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1
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2
1
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694428
Araiso
Structural insights into RNA-d ...
Methanococcus maripaludis
Nucleic Acids Res.
36
1187-1199
2008
-
-
1
1
5
-
-
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1
-
5
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1
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2
1
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1
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1
1
1
5
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1
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1
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2
1
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694847
Yuan
RNA-dependent conversion of ph ...
Homo sapiens, Methanocaldococcus jannaschii, Methanococcus maripaludis
Proc. Natl. Acad. Sci. USA
103
18923-18927
2006
-
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3
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3
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10
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3
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6
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3
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3
3
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3
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3
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6
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