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Literature summary for 2.7.7.72 extracted from

  • Cho, H.D.; Verlinde, C.L.; Weiner, A.M.
    Archaeal CCA-adding enzymes: central role of a highly conserved beta-turn motif in RNA polymerization without translocation (2005), J. Biol. Chem., 280, 9555-9566.
    View publication on PubMed
Search for more literature for 2.7.7.72

Protein Variants

Protein Variants Comment Organism
E92F the mutant is nearly inactive for CCA addition, although tRNA binding is apparently normal Saccharolobus shibatae
G166R C74-adding is 7% of wild-type activity, C75-adding is 8% of wild-type activity, A76-adding is 21% of wild-type activity Saccharolobus shibatae
G169R C74-adding is 5% of wild-type activity, C75-adding is 2% of wild-type activity, A76-adding is 22% of wild-type activity Saccharolobus shibatae
H129A C74-adding is 22% of wild-type activity, C75-adding is 28% of wild-type activity, A76-adding is 87% of wild-type activity Saccharolobus shibatae
H93V the mutant adds C74 and C75 but fails to add A76 Saccharolobus shibatae
H93V/Y95V the mutant enzyme is completely inactive for CCA addition Saccharolobus shibatae
K149A no C74-adding activity, C75-adding is 1% of wild-type activity, A76-adding is 1% of wild-type activity Saccharolobus shibatae
K153A C74-adding is 14% of wild-type activity, C75-adding is 4% of wild-type activity, A76-adding is 3% of wild-type activity Saccharolobus shibatae
additional information mutations near the active site can differentially affect addition of C74, C75, or A76 Saccharolobus shibatae
R125A C74-adding is 30% of wild-type activity, C75-adding is 10% of wild-type activity, A76-adding is 5% of wild-type activity Saccharolobus shibatae
Y158A C74-adding is 9% of wild-type activity, C75-adding is 15% of wild-type activity, A76-adding is 7% of wild-type activity Saccharolobus shibatae
Y90E the mutant is nearly wild type for CCA addition despite replacement of a conserved bulky hydrophobic residue by a carboxylate Saccharolobus shibatae
Y90E/E92F the mutant enzyme is completely inactive for CCA addition Saccharolobus shibatae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.015
-
 CTP pH 9.0, 70°C, wild-type enzyme Saccharolobus shibatae
0.02
-
 CTP pH 9.0, 70°C, mutant enzyme R125A Saccharolobus shibatae
0.03
-
 CTP pH 9.0, 70°C, mutant enzyme E92F Saccharolobus shibatae
0.033
-
 CTP pH 9.0, 70°C, mutant enzyme Y158A Saccharolobus shibatae
0.04
-
 CTP pH 9.0, 70°C, mutant enzyme H129A Saccharolobus shibatae
0.057
-
 CTP pH 9.0, 70°C, mutant enzyme K153A Saccharolobus shibatae
0.062
-
 CTP pH 9.0, 70°C, mutant enzyme Y90E/E92F Saccharolobus shibatae
0.067
-
 CTP pH 9.0, 70°C, mutant enzyme H93V/Y95V Saccharolobus shibatae
0.1
-
 CTP pH 9.0, 70°C, mutant enzyme G166R Saccharolobus shibatae
0.142
-
 CTP pH 9.0, 70°C, mutant enzyme G169R Saccharolobus shibatae
0.167
-
 CTP pH 9.0, 70°C, mutant enzyme K149A Saccharolobus shibatae

Organism

Organism UniProt Comment Textmining
Saccharolobus shibatae P77978
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
a tRNA precursor + 2 CTP + ATP overall reaction Saccharolobus shibatae a tRNA with a 3' CCA end + 3 diphosphate
-
 ?
a tRNA precursor + CTP
-
 Saccharolobus shibatae a tRNA with a 3' cytidine end + diphosphate
-
 ?
a tRNA with a 3' CC end + ATP
-
 Saccharolobus shibatae a tRNA with a 3' CCA end + diphosphate
-
 ?
a tRNA with a 3' cytidine + CTP
-
 Saccharolobus shibatae a tRNA with a 3' CC end + diphosphate
-
 ?

Synonyms

Synonyms Comment Organism
CCA-adding enzyme
-
 Saccharolobus shibatae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
 assay at Saccharolobus shibatae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
 assay at Saccharolobus shibatae