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2.4.2.29: tRNA-guanosine34 preQ1 transglycosylase

This is an abbreviated version!
For detailed information about tRNA-guanosine34 preQ1 transglycosylase, go to the full flat file.

Word Map on EC 2.4.2.29

Reaction

guanine34 in tRNA
+
7-aminomethyl-7-carbaguanine
=
7-aminomethyl-7-carbaguanine34 in tRNA
+
guanine

Synonyms

ArcTGT, guanine insertion enzyme, guanine, queuine-tRNA transglycosylase, Q-insertase, QTRT1, QueTGT, queuine insertase, queuine tRNA ribosyltransferase, queuine tRNA-ribosyltransferase, queuine tRNA-ribosyltransferase subunit 1, ribosyltransferase, queuine transfer ribonucleate, TGT, transfer ribonucleate glycosyltransferase, tRNA guanine transglycosidase, tRNA guanine transglycosylase, tRNA transglycosylase, tRNA-guanine 34 transglycosylase, tRNA-guanine transglycosylase, tRNA–guanine transglycosylase, virulence-associated protein VACC

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.29 tRNA-guanosine34 preQ1 transglycosylase

Engineering

Engineering on EC 2.4.2.29 - tRNA-guanosine34 preQ1 transglycosylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D264N
-
is inactive and incapable of forming the covalent intermediate, while maintaining the ability to bind noncovalently to RNA
D89A
-
less than 1% of the activity of the histidine-tagged wild-type enzyme
D89C
-
less than 1% of the activity of the histidine-tagged wild-type enzyme
D89E
-
about 50% of the activity of the histidine-tagged wild-type enzyme
D89N
-
less than 1% of the activity of the histidine-tagged wild-type enzyme
S90A
-
activity of the mutant enzyme is to low to determine Vmax and Km-value
S90C
-
30fold increase in Km-value for tRNATyr and 4fold increase in Km-value for guanine
S90F
-
mutant enzyme has no detectable solubility and reduced solubility
E235Q
the mutation has no significant influence on kcat, but Km for preQ1 is drastically increased, while Km for preQ0 seems to be decreased
K52M
reduced turnover value. At a concentration of protein of 0.01 mM appears almost exclusively as a homodimer as the wild-type, when the concentration of protein is lowered to a minimal value of 0.001 mM, a substantial proportion of monomer becomes evident
Y106F
crystallises similarly to the wild-type
Y330F
reduced turnover value. At a concentration of protein of 0.01 mM reveals a significant amount of monomer, when the concentration of protein is lowered to a minimal value of 0.001 mM, a substantial proportion of monomer becomes evident