6.5.1.3: RNA ligase (ATP)
This is an abbreviated version!
For detailed information about RNA ligase (ATP), go to the full flat file.
Word Map on EC 6.5.1.3
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6.5.1.3
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trna
-
polynucleotide
-
ligases
-
phosphodiester
-
termini
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rnase
-
brucei
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single-stranded
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oligoribonucleotides
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3'-terminal
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adenylylation
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3'-phosphate
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5\'-hydroxyl
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kinetoplastids
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anticodons
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aminoacylation
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nucleotidyl
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3',5'-bisphosphate
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rlm-race
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nucleotidyltransferase
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trnaphe
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3',5'-phosphodiester
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uridylate
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5'-phosphorylated
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viroid
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editosome
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3'-phosphodiesterase
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tarentolae
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t4-induced
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half-molecules
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splint
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hammerhead
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trnafmet
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rolling-circle
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deoxyribozymes
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tutase
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template-directed
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t4-infected
-
5\'-half
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medicine
-
synthesis
-
molecular biology
- 6.5.1.3
- trna
- polynucleotide
- ligases
-
phosphodiester
- termini
- rnase
- brucei
-
single-stranded
- oligoribonucleotides
-
3'-terminal
-
adenylylation
- 3'-phosphate
-
5\'-hydroxyl
- kinetoplastids
-
anticodons
- aminoacylation
-
nucleotidyl
-
3',5'-bisphosphate
-
rlm-race
-
nucleotidyltransferase
- trnaphe
-
3',5'-phosphodiester
-
uridylate
-
5'-phosphorylated
- viroid
-
editosome
- 3'-phosphodiesterase
- tarentolae
-
t4-induced
-
half-molecules
-
splint
-
hammerhead
- trnafmet
-
rolling-circle
-
deoxyribozymes
-
tutase
-
template-directed
-
t4-infected
-
5\'-half
- medicine
- synthesis
- molecular biology
Reaction
Synonyms
ATP-dependent RNA ligase, b1-10t, bacteriophage RNA ligase, band IV protein, class I ligase, class I RNA ligase ribozyme, DraRnI, DraRnl, DREL, gp24.1, P52, phage Rnl2, Polynucleotide synthetase, Polyribonucleotide ligase, Polyribonucleotide synthase (ATP), REL1, Ribonucleic ligase, ribonucleprotein editing complex, RM378 RNA ligase, RNA editing ligase 1, RNA ligase, RNA ligase (ATP), RNA ligase 1, RNA ligase 2, RNA ligase ribozyme, RNA-editing ligase 1, RNL, Rnl1, Rnl2, Rnl5, RnlA, RtcA, rtcB, Synthetase, polyribonucleotide, T4 RNA ligase, T4 RNA ligase 1, T4 RNA ligase 2, T4Rnl2, TbMP52, TbREL1, thermostable RNA ligase 1, Trl1
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Metals Ions
Metals Ions on EC 6.5.1.3 - RNA ligase (ATP)
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Mg2+
Mn2+
additional information
Mg2+
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L1 ligase is an obligate metalloenzyme that is highly specific for Mg2+. It is selected in the presence of 60 mM MgCl2 and functions optimally in Mg2+ concentrations as high as 100 mM
Mg2+
Tequatrovirus T4
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the active site contains two metal ions, consistent with the two-magnesium ion catalytic mechanism
Mg2+
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magnesium ion interacts with the beta and gamma-phosphate groups and is almost perfectly octahedrally coordinated by six phosphate and water oxygen atoms
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calcium, cobalt, copper, cadmium, nickel, and zinc are ineffective
additional information
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no detectable activity with Ca2+, Sr2+, Ba2+, Zn2+, Co2+, Cd2+, Pb2+, Co(NH3)6 3+, or spermine