2.7.1.164: O-phosphoseryl-tRNASec kinase
This is an abbreviated version!
For detailed information about O-phosphoseryl-tRNASec kinase, go to the full flat file.
Word Map on EC 2.7.1.164
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2.7.1.164
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selenocysteine
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selenoproteins
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sep-trna:sec-trna
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selenophosphate
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jannaschii
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sepsecs
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decoding
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serylates
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ser-trnasec
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methanocaldococcus
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methanococcus
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anticodon
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aminoacylated
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trna-dependent
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selenide
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selenocysteine-specific
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selenocysteinyl-trna
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eukarya
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trnasersec
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aminoacyl-trnas
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maripaludis
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d-stem
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aa-trnas
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amidotransferases
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amppnp
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trnaser
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misacylated
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serrs
- 2.7.1.164
- selenocysteine
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selenoproteins
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sep-trna:sec-trna
- selenophosphate
- jannaschii
- sepsecs
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decoding
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serylates
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ser-trnasec
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methanocaldococcus
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methanococcus
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anticodon
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aminoacylated
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trna-dependent
- selenide
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selenocysteine-specific
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selenocysteinyl-trna
- eukarya
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trnasersec
- aminoacyl-trnas
- maripaludis
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d-stem
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aa-trnas
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amidotransferases
- amppnp
- trnaser
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misacylated
- serrs
Reaction
Synonyms
O-phosphoseryl-tRNA kinase, O-phosphoseryl-tRNA(Sec) kinase, O-phosphoseryl-tRNASec kinase, phosphoseryl-tRNASec kinase, phosphoseryl-tRNA[Ser]Sec kinase, PSTK, Tb10.6k15.1110, TbPSTK
ECTree
2.7.1.164 O-phosphoseryl-tRNASec kinaseAdvanced search results
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results (Engineering
Engineering on EC 2.7.1.164 - O-phosphoseryl-tRNASec kinase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
K142A/Y143A
mutant shows severely reduced activity with the Methanopyrus kandleri tRNASec substrate
K17A
R116A
mutant enzyme is 23.5fold less active than wild-type enzyme
S18A
T19W
mutant enzyme is 2.8fold less active than wild-type enzyme
R116A
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mutant enzyme is 23.5fold less active than wild-type enzyme
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S18A
T19W
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mutant enzyme is 2.8fold less active than wild-type enzyme
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additional information
K17A
mutation abolishes catalytic activity and and inhibits tRNASec recognition
S18A
mutation abolishes catalytic activity and and inhibits tRNASec recognition
S18A
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mutation abolishes catalytic activity and and inhibits tRNASec recognition
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additional information
truncation of the C-termional domain. Deletions of up to 98 amino acids, PSTK1-153, still show activity, albeit at a much reduced level of about 6% of the initial velocity of the intact enzyme. In vivo, PSTK1-153 is still able compensate for the Escherichia coli selA deletion. Truncation PSTK1-192 lacks the entire CTD domain and exhibits 40% residual activity. PSTK1-215 and PSTK1-240 mutants lack the terminal two and one helices of the helix bundle, respectively. PSTK1-215 mutant shows remarkably reduced activity
additional information
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truncation of the C-termional domain. Deletions of up to 98 amino acids, PSTK1-153, still show activity, albeit at a much reduced level of about 6% of the initial velocity of the intact enzyme. In vivo, PSTK1-153 is still able compensate for the Escherichia coli selA deletion. Truncation PSTK1-192 lacks the entire CTD domain and exhibits 40% residual activity. PSTK1-215 and PSTK1-240 mutants lack the terminal two and one helices of the helix bundle, respectively. PSTK1-215 mutant shows remarkably reduced activity
additional information
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truncation of the C-termional domain. Deletions of up to 98 amino acids, PSTK1-153, still show activity, albeit at a much reduced level of about 6% of the initial velocity of the intact enzyme. In vivo, PSTK1-153 is still able compensate for the Escherichia coli selA deletion. Truncation PSTK1-192 lacks the entire CTD domain and exhibits 40% residual activity. PSTK1-215 and PSTK1-240 mutants lack the terminal two and one helices of the helix bundle, respectively. PSTK1-215 mutant shows remarkably reduced activity
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