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Literature summary for 3.1.3.32 extracted from

  • Martins, A.; Shuman, S.
    Characterization of a baculovirus enzyme with RNA ligase, polynucleotide 5'-Kinase, and polynucleotide 3'-phosphatase activities (2004), J. Biol. Chem., 279, 18220-18231.
    View publication on PubMed
Search for more literature for 3.1.3.32

Cloned(Commentary)

Cloned (Comment) Organism
wild-type C-terminal domain Rnl1-(394-694) and mutated versions K407A and D560A are produced in Escherichia coli as a His10 fusion. The end-healing domain Rnl1-(394-694) consists of a proximal 5'-kinase module with an essential P-loop motif (404GSGKS408) and a distal 3'-phosphatase module with an essential acylphosphatase motif (560DLDGT564) unidentified baculovirus

Protein Variants

Protein Variants Comment Organism
D560A mutation abolishes phosphatase activity of the C-terminal domain Rnl1-(394-694) unidentified baculovirus
K407A mutation has no effect on phosphatase activity of the C-terminal domain Rnl1-(394-694) unidentified baculovirus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ divalent cation required, activity is proportional to Mg2+ concentration in the range of 0-0.3 mM and reach a plateau at 0.6-5 mM unidentified baculovirus

Organism

Organism UniProt Comment Textmining
unidentified baculovirus
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Purification (Commentary)

Purification (Comment) Organism
wild-type C-terminal domain Rnl1-(394-694) and mutated versions K407A and D560A, produced in Escherichia coli as a His10 fusion unidentified baculovirus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
d(TTTAATCAATTGCGACCCp) + H2O reaction with the end-healing domain Rnl1-(394-694), that consists of a proximal 5'-kinase module with an essential P-loop motif (404GSGKS408) and a distal 3'-phosphatase module with an essential acylphosphatase motif (560DLDGT564) unidentified baculovirus phosphate + d(TTTAATCAATTGCGACCC)
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 ?

Synonyms

Synonyms Comment Organism
RNA ligase 1 trifunctional enzyme catalzes RNA ligase, polynucleotide 5'-kinase, and polynucleotide 3'-phosphatase activities. The end-healing domain Rnl1-(394-694) consists of a proximal 5'-kinase module with an essential P-loop motif (404GSGKS408) and a distal 3'-phosphatase module with an essential acylphosphatase motif (560DLDGT564) unidentified baculovirus
Rnl1 trifunctional enzyme catalzes RNA ligase, polynucleotide 5'-kinase, and polynucleotide 3'-phosphatase activities. The end-healing domain Rnl1-(394-694) consists of a proximal 5'-kinase module with an essential P-loop motif (404GSGKS408) and a distal 3'-phosphatase module with an essential acylphosphatase motif (560DLDGT564) unidentified baculovirus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
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 reaction with the end-healing domain Rnl1-(394-694) unidentified baculovirus

pH Range

pH Minimum pH Maximum Comment Organism
5 7.5 pH 5.0: about 30% of maximal activity, pH 7.5: about 35% of maximal activity, reaction with the end-healing domain Rnl1-(394-694) unidentified baculovirus