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2.7.7.B5: adenylyltransferase ThiI

This is an abbreviated version!
For detailed information about adenylyltransferase ThiI, go to the full flat file.

Reaction

tRNA-uridine
+
ATP
=
adenylated-tRNA-uridine
+
diphosphate

Synonyms

ThiI

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.B5 adenylyltransferase ThiI

Engineering

Engineering on EC 2.7.7.B5 - adenylyltransferase ThiI

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D189A
-
mutation eliminates in vivo function of the enzyme
K321M
-
mutation eliminates in vivo function of the enzyme
C207S
-
using a complementation assay it is shown that mutant is required for 4-thiouridine synthesis but not for thiazole synthesis
C344S
-
using a complementation assay it is shown that mutant is required for 4-thiouridine synthesis but not for thiazole synthesis
C456S
-
using a complementation assay it is shown that mutant is required for 4-thiouridine synthesis and for thiazole synthesis
D189A
-
using a complementation assay it is shown that mutant is required for 4-thiouridine synthesis but not for thiazole synthesis
K321M
-
using a complementation assay it is shown that mutant is required for 4-thiouridine synthesis but not for thiazole synthesis
additional information
-
construction of two truncated forms of ThiI containing the N-terminal domain including NFLD and THUMP, and the C-terminal domain including the PP-loop and RLD domains, respectively. The N-domain can bind with both tRNAPhe and TPHE39A and recognizes the acceptor-stem region, whereas the C-domain cannot. The C-domain also affects RNA binding by its enthalpically favorable, but entropically unfavorable, contribution. The C-domain induces a conformation change in tRNAPhe