6.5.1.8: 3'-phosphate/5'-hydroxy nucleic acid ligase
This is an abbreviated version!
For detailed information about 3'-phosphate/5'-hydroxy nucleic acid ligase, go to the full flat file.
Reaction
Synonyms
3'-P RNL, MXAN_0280, MXAN_4982, RNA-splicing ligase, rtcB, RtcB RNA ligase, Rtcb-1, RtcB1, Trl1, tRNA splicing ligase, tRNA-splicing ligase
ECTree
6.5.1.8 3'-phosphate/5'-hydroxy nucleic acid ligaseAdvanced search results
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results (Engineering
Engineering on EC 6.5.1.8 - 3'-phosphate/5'-hydroxy nucleic acid ligase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C78A
D75A
H168A
H185A
H280A
active, protein is able to complement a Saccharomyces cerevisiae Trl1 mutant
H281A
-
the mutant is impaired in overall 5'-OH-RNAp and 5'-OH-RNA-2',3'-cyclic phosphate ligation but is able to seal a preguanylylated substrate
H337A
H337N
H337Q
K299A
-
the mutant shows about 50% of 5'-OH-RNAp ligation activity compared to the wild type enzyme
N167A
R189A
R341A
R345A
-
the mutant shows 5'-OH-RNAp ligation activity similar to the wild type enzyme
D75A
-
the mutation allows cyclic phosphodiester hydrolysis but cripples 3'-phosphate guanylylation
H168A
-
the mutant shows about 48% of 5'-OH-RNAp ligation activity compared to the wild type enzyme
H185A
-
the mutant shows 5'-OH-RNAp ligation activity similar to the wild type enzyme
H337A
His337 is the site covalent guanylylation of RtcB, mutant is inactive
H337A
residue His337 is the site of covalent guanylylation, the mutation abolishes 3'-phosphate/5'-OH RNA ligation
H337A
-
the mutant shows about 1% of 5'-OH-RNAp ligation activity compared to the wild type enzyme
H337N
residue His337 is the site of covalent guanylylation, the mutation abolishes 3'-phosphate/5'-OH RNA ligation
H337Q
residue His337 is the site of covalent guanylylation, the mutation abolishes 3'-phosphate/5'-OH RNA ligation
N167A
-
the mutant shows about 65% of 5'-OH-RNAp ligation activity compared to the wild type enzyme
R189A
-
the mutation slows the step of RNAppG/5'-OH RNA sealing by a factor of 200 compared to that with wild type enzyme while decreasing the rate of RNAppG formation by 3fold
R341A
-
the mutant shows about 10% of 5'-OH-RNAp ligation activity compared to the wild type enzyme
