Information on EC 2.1.1.216 - tRNA (guanine26-N2)-dimethyltransferase

Word Map on EC 2.1.1.216
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
2.1.1.216
-
RECOMMENDED NAME
GeneOntology No.
tRNA (guanine26-N2)-dimethyltransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 S-adenosyl-L-methionine + guanine26 in tRNA = 2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
NIL
-
-
tRNA methylation (yeast)
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (guanine26-N2)-dimethyltransferase
The enzyme dissociates from its tRNA substrate between the two consecutive methylation reactions. In contrast to EC 2.1.1.215, tRNA (guanine26-N2/guanine27-N2)-dimethyltransferase, this enzyme does not catalyse the methylation of guanine27 in tRNA.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
little changes occur in the relative levels of different tRNAs in maf1DELTA cells. By contrast, the efficiency of N2,N2-dimethyl G26 modification on certain tRNAs is decreased in response to maf1-deletion and is associated with antisuppression
metabolism
-
global tRNA gene activation occurs with derepression of RNA polymerase III via maf1-deletion and is accompanied by a paradoxical loss of tRNA-mediated nonsense suppressor activity, manifested as an antisuppression phenotype. maf1-Antisuppression also occurs in the fission yeast amidst general activation of RNA polymerase III. Dimethyl-guanine-26 varies in the efficiency by which it is added to its target tRNAs, in a manner that is dependent on the overall activity rate of RNA polyymerase III. Overexpression of Trm1, which produces the N2,N2-dimethyl G26 modification, reverses maf1-antisuppression. Competition by increased tRNA levels in maf1DELTA cells leads to N2,N2-dimethyl G26 hypomodification due to limiting Trm1, reducing the activity of suppressor-tRNASerUCA and accounting for antisuppression
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + guanine26 in elongator tRNAMet
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in elongator tRNAMet
show the reaction diagram
2 S-adenosyl-L-methionine + guanine26 in initiator tRNAMet
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in initiator tRNAMet
show the reaction diagram
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 tRNA
show the reaction diagram
2 S-adenosyl-L-methionine + guanine26 in tRNALeu(UAG)
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeu(UAG)
show the reaction diagram
-
-
-
?
2 S-adenosyl-L-methionine + guanine26 in tRNAPhe
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 tRNAPhe
show the reaction diagram
4 S-adenosyl-L-methionine + guanine26 in initiator tRNAMet
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in initiator tRNAMet
show the reaction diagram
4 S-adenosyl-L-methionine + guanine26 in prolongator tRNAMet
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in prolongator tRNAMet
show the reaction diagram
4 S-adenosyl-L-methionine + guanine26 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
show the reaction diagram
4 S-adenosyl-L-methionine + guanine26 in tRNALeuCAA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeuCAA
show the reaction diagram
-
-
-
-
?
4 S-adenosyl-L-methionine + guanine26 in tRNALeuTAG
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeuTAG
show the reaction diagram
-
-
-
-
?
4 S-adenosyl-L-methionine + guanine26 in tRNASerUCA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNASerUCA
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine26 in elongator tRNAMet
S-adenosyl-L-homocysteine + N2-methylguanine26 in elongator tRNAMet
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + guanine26 in initiator tRNAMet
S-adenosyl-L-homocysteine + N2-methylguanine26 in initiator tRNAMet
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
show the reaction diagram
S-adenosyl-L-methionine + guanine26 in tRNAPhe
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNAPhe
show the reaction diagram
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
show the reaction diagram
S-adenosyl-L-methionine + N2-methylguanine26 in tRNAPhe
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNAPhe
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + guanine26 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 tRNA
show the reaction diagram
-
the efficient dimethylation of guanine26 requires the presence of base-pairs C11*G24 and G10*C25 and a variable loop of five bases within a correct 3D-core of the tRNA molecule. These identity elements probably ensure the correct presentation of methylated m2G26 to the enzyme for the attachment of the second methyl group
-
-
?
4 S-adenosyl-L-methionine + guanine26 in initiator tRNAMet
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in initiator tRNAMet
show the reaction diagram
4 S-adenosyl-L-methionine + guanine26 in prolongator tRNAMet
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in prolongator tRNAMet
show the reaction diagram
4 S-adenosyl-L-methionine + guanine26 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
show the reaction diagram
4 S-adenosyl-L-methionine + guanine26 in tRNALeuCAA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeuCAA
show the reaction diagram
-
-
-
-
?
4 S-adenosyl-L-methionine + guanine26 in tRNALeuTAG
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNALeuTAG
show the reaction diagram
-
-
-
-
?
4 S-adenosyl-L-methionine + guanine26 in tRNASerUCA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNASerUCA
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine26 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26 in tRNA
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in tRNA
show the reaction diagram
-
the efficient dimethylation of guanine26 requires the presence of base-pairs C11*G24 and G10*C25 and a variable loop of five bases within a correct 3D-core of the tRNA molecule. These identity elements probably ensure the correct presentation of methylated m2G26 to the enzyme for the attachment of the second methyl group
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
the efficiency of N2,N2-dimethyl G26 modification on certain tRNAs is decreased in response to maf1-deletion and is associated with antisuppression
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Rapamycin
-
a decrease in tRNA synthesis by treatment with rapamycin leads to increased N2,N2-dimethyl G26 modification
additional information
-
RNA polymerase III mutations associated with hypomyelinating leukodystrophy decrease tRNA transcription, increase of N2,N2-dimethyl G26 modification efficiency and reverse antisuppression
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003
S-adenosyl-L-methionine
-
pH 7.2, 50°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.7
calculated from sequence
9.2
-
calculated from sequence
PDB
SCOP
CATH
ORGANISM
UNIPROT
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43300
calculated from sequence
45700
-
calculated from sequence
49000
-
gel filtration
58400
calculated from sequence
64050
-
calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop method, crystal structures of Trm1 from Pyrococcus horikoshii liganded with S-adenosyl-l-methionine or S-adenosyl-l-homocysteine
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
-
2 h: stable
90
-
2 h: 30% loss of activity
95
-
t1/2: 2 h
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, the enzyme precipitates if stored for several days
-
4°C, the purified enzyme can be stored for several months without loss of activity
-
frozen in small portions, enzyme maintains activity for at least several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native and mutant Trm1 proteins
recombinant enzyme (pfTrm1p) with a His6-tag at the N-terminus
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli and the His-tagged Trm1 protein
-
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R246A
more than 97% loss of activity
R246G
mutation eliminates the methylation activity
E47A
-
mutant enzyme shows 6% of wild-type activity
G48A
-
mutant enzyme shows 16% of wild-type activity
K290A
-
mutant enzyme loses 56% of its methylation activity
S467L
-
complete loss of enzyme activity in vitro against trm1 yeast tRNA
S570A
-
fully active mutant enzyme
additional information
-
comparatively short N- or C-terminal deletions from the 570 amino acid long Trm1 polypeptide decreased or eliminated the enzyme activity. The first 27 N-terminal amino acids in rTrmp1 are not needed for G26 modification activity in vitro or in vivo. DELTAC5aa causes the in vitro modification activity to drastically decrease to 27% of the wild-type rate. Additional deletions up to DELTA30aa further lower the activity to about 7% of the wild-type value. In DELTA10aa an increase of the N2-methylguanine26 relative to N2-dimethylguanine26 tRNA is observed, but with further C-terminal deletions the monomethylation activity is also severely lowered
Show AA Sequence (366 entries)
Please use the Sequence Search for a certain query.