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Literature summary for 2.7.7.79 extracted from

  • Hyde, S.J.; Rao, B.S.; Eckenroth, B.E.; Jackman, J.E.; Doublie, S.
    Structural studies of a bacterial tRNA(HIS) guanylyltransferase (Thg1)-like protein, with nucleotide in the activation and nucleotidyl transfer sites (2013), PLoS ONE, 8, e67465.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.79

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bacillus thuringiensis serovar israelensis

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with ATP and with GTP. The enzyme is a tetramer. Catalysis of the 3'-5' reaction with 5'-monophosphorylated tRNA necessitates first an activation step, generating a 5'-adenylylated intermediate prior to a second nucleotidyl transfer step, in which a nucleotide is transferred to the tRNA 5'-end. Distinct binding sites are observed for the nucleotides involved in these two steps Bacillus thuringiensis serovar israelensis

Protein Variants

Protein Variants Comment Organism
K43A the observed rate of adenylylation is decreased by about 10fold, while the rate of guanylylation is virtually unchanged Bacillus thuringiensis serovar israelensis
M158A no effect on the observed rate of activation Bacillus thuringiensis serovar israelensis
M158N mutation does not impart the preference for ATP to the enzyme, but it further improves the kinetics for GTP-dependent activation by 10fold relative to the wild-type Bacillus thuringiensis serovar israelensis

Organism

Organism UniProt Comment Textmining
Bacillus thuringiensis serovar israelensis Q3F0V8
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Bacillus thuringiensis serovar israelensis ATCC 35646 Q3F0V8
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information when full-length tRNAHis (lacking the G-1 residue) is used as a substrate, TLP exhibits a strong preference for use of GTP over ATP for 5'-end activation. Product formation is extremely slow in the presence of only ATP. With a 5'-truncated substrate missing the +1 nucleotide, both ATP and GTP are used with relatively equal efficiency for activation Bacillus thuringiensis serovar israelensis ?
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 ?
additional information when full-length tRNAHis (lacking the G-1 residue) is used as a substrate, TLP exhibits a strong preference for use of GTP over ATP for 5'-end activation. Product formation is extremely slow in the presence of only ATP. With a 5'-truncated substrate missing the +1 nucleotide, both ATP and GTP are used with relatively equal efficiency for activation Bacillus thuringiensis serovar israelensis ATCC 35646 ?
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 ?
p-tRNAHis + ATP
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 Bacillus thuringiensis serovar israelensis App-tRNAHis + diphosphate
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 ?
p-tRNAHis + ATP
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 Bacillus thuringiensis serovar israelensis ATCC 35646 App-tRNAHis + diphosphate
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 ?
p-tRNAHis + ATP + GTP
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 Bacillus thuringiensis serovar israelensis pppGp-tRNAHis + AMP + diphosphate overall reaction ?
p-tRNAHis + ATP + GTP
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 Bacillus thuringiensis serovar israelensis ATCC 35646 pppGp-tRNAHis + AMP + diphosphate overall reaction ?

Synonyms

Synonyms Comment Organism
RBTH_06728
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 Bacillus thuringiensis serovar israelensis