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Information on EC 2.1.1.216 - tRNA (guanine26-N2)-dimethyltransferase and Organism(s) Pyrococcus horikoshii and UniProt Accession O59493

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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.216 tRNA (guanine26-N2)-dimethyltransferase
IUBMB Comments
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.
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This record set is specific for:
Pyrococcus horikoshii
UNIPROT: O59493
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Word Map
The taxonomic range for the selected organisms is: Pyrococcus horikoshii
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Reaction Schemes
Synonyms
trm1p, zc376.5, ta0997, trna (m22g26)dimethyltransferase, trm1 methyltransferase, more
PATHWAY SOURCE
PATHWAYS
-
-
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.
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 tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine26 tRNA
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
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native and mutant Trm1 proteins
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ihsanawati; Nishimoto, M.; Higashijima, K.; Shirouzu, M.; Grosjean, H.; Bessho, Y.; Yokoyama, S.
Crystal Structure of tRNA N(2),N(2)-Guanosine Dimethyltransferase Trm1 from Pyrococcus horikoshii
J. Mol. Biol.
383
871-884
2008
Pyrococcus horikoshii (O59493)
Manually annotated by BRENDA team