Literature summary for 2.7.7.52 extracted from

Cheng, L.; Li, F.; Jiang, Y.; Yu, H.; Xie, C.; Shi, Y.; Gong, Q.
Structural insights into a unique preference for 3 terminal guanine of mirtron in Drosophila TUTase Tailor (2019), Nucleic Acids Res., 47, 495-508 .

Search for more literature for 2.7.7.52

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli Gold (DE3) cells	Drosophila melanogaster

Crystallization (Commentary)

Crystallization (Comment)	Organism
enzyme residues 202-560 and enzyme in complex with RNA stretches 5 -AGU-3 and 5 -AGUU-3 , sitting drop vapor diffusion method, using 0.1 M Tris-HCl, pH 8.4, 50 mM NaCl, 0.2 M lithium sulfate monohydrate and 15% (w/v) PEG3350	Drosophila melanogaster

Protein Variants

Protein Variants	Comment	Organism
H294A	the enzymatic activity of the mutant is reduced by about 61% as compared to the wild type enzyme	Drosophila melanogaster
N347A	the uridylation efficiency of the mutant is reduced dramatically to about 7% when compared with that of wild type enzyme	Drosophila melanogaster
R295A	the enzymatic activity of the mutant is reduced by about 84% as compared to the wild type enzyme	Drosophila melanogaster
R295K	the enzymatic activity of the mutant is reduced by about 80% as compared to the wild type enzyme	Drosophila melanogaster
R327A	the uridylation efficiency of the mutant is reduced dramatically to about 4% when compared with that of wild type enzyme	Drosophila melanogaster
R327K	the uridylation efficiency of the mutant is reduced dramatically to about 4% when compared with that of wild type enzyme	Drosophila melanogaster
V328I	the mutation barely affects the enzyme's binding with RNA substrate and also exhibits a obvious reduction in uridylation efficiency as compared to the wild type enzyme	Drosophila melanogaster
V328L	the mutation entirely abolishes the enzyme's catalytic activity for truncated miR-1003 bearing 3'G. The mutation barely affects the enzyme's binding with RNA substrate	Drosophila melanogaster
V328R	the mutation entirely abolishes the enzyme's catalytic activity for truncated miR-1003 bearing 3'G. The mutation barely affects the enzyme's binding with RNA substrate	Drosophila melanogaster

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Drosophila melanogaster

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
UTP + miR-1003 RNAn	Drosophila melanogaster	-	diphosphate + miR-1003 RNAn+1	-	?
UTP + RNAn	Drosophila melanogaster	the enzyme exhibits an intrinsic preference for RNA substrates ending in 3'G	diphosphate + RNAn+1	-	?

Organism

Organism	UniProt	Comment	Textmining
Drosophila melanogaster	Q9VI58	-	-

Purification (Commentary)

Purification (Comment)	Organism
Ni-NTA column chromatography, HiTrap heparin column chromatography and Superdex 200 gel filtration	Drosophila melanogaster

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
UTP + 5'-Cy5-GUGGGUAUCUGGGAGAUUACAUAUUCACAG-3'	-	Drosophila melanogaster	?	-	?
UTP + 5-Cy5-CAUAUUCACAG-3'	-	Drosophila melanogaster	?	-	?
UTP + miR-1003 RNAn	-	Drosophila melanogaster	diphosphate + miR-1003 RNAn+1	-	?
UTP + mirtronRNAn	the enzyme preferentially catalyzes the uridylation of mirtronRNAs ending in 3'G and 3'U	Drosophila melanogaster	diphosphate + mirtronRNAn+1	-	?
UTP + RNAn	the enzyme exhibits an intrinsic preference for RNA substrates ending in 3'G	Drosophila melanogaster	diphosphate + RNAn+1	-	?

Synonyms

Synonyms	Comment	Organism
Tailor	-	Drosophila melanogaster
terminal uridylyl transferase	-	Drosophila melanogaster
TUTase	-	Drosophila melanogaster

General Information

General Information	Comment	Organism
metabolism	the enzyme plays a crucial role as the repressor in the biogenesis pathway of splicing-derived mirtron pre-miRNAs	Drosophila melanogaster

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Release 2023.1 (January 2023)