Literature summary for 2.7.7.72 extracted from

Ernst, F.G.; Rickert, C.; Bluschke, A.; Betat, H.; Steinhoff, H.J.; Moerl, M.
Domain movements during CCA-addition: a new function for motif C in the catalytic core of the human tRNA nucleotidyltransferases (2015), RNA Biol., 12, 435-446.

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Protein Variants

Protein Variants	Comment	Organism
D139A	mutant shows a strong reduction in the addition of the terminal A position	Homo sapiens
G143A	similar to wild-type, mutant catalyzes the addition of the complete CCA sequence	Homo sapiens
R153A	similar to wild-type, mutant catalyzes the addition of the complete CCA sequence	Homo sapiens

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.008	-	a tRNA precursor	mutant D139A, pH not specified in the publication, temperature not specified in the publication	Homo sapiens
0.119	-	a tRNA precursor	wild-type, pH not specified in the publication, temperature not specified in the publication	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	-	Homo sapiens	5739	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q96Q11	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
a tRNA precursor + 2 CTP + ATP	-	Homo sapiens	a tRNA with a 3' CCA end + 3 diphosphate	-	?

Synonyms

Synonyms	Comment	Organism
TRNT1	-	Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.09	-	a tRNA precursor	wild-type, pH not specified in the publication, temperature not specified in the publication	Homo sapiens
0.11	-	a tRNA precursor	mutant D139A, pH not specified in the publication, temperature not specified in the publication	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	conserved motif C in CCA-adding enzyme forms a flexible spring element modulating the relative orientation of the enzyme's head and body domains to accommodate the growing 3'-end of the tRNA. These conformational transitions initiate the rearranging of the templating amino acids to switch the specificity of the nucleotide binding pocket from CTP to ATP during CCA-synthesis	Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
0.07	-	a tRNA precursor	mutant D139A, pH not specified in the publication, temperature not specified in the publication	Homo sapiens
1.23	-	a tRNA precursor	wild-type, pH not specified in the publication, temperature not specified in the publication	Homo sapiens

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Release 2023.1 (January 2023)