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Information on EC 2.1.1.216 - tRNA (guanine26-N2)-dimethyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P15565

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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:
Saccharomyces cerevisiae
UNIPROT: P15565
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Archaea
Reaction Schemes
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2
S-adenosyl-L-methionine
+
guanine26 in tRNA
=
2
S-adenosyl-L-homocysteine
+
N2-dimethylguanine26 in tRNA
2
+
guanine26 in tRNA
=
2
+
N2-dimethylguanine26 in tRNA
Synonyms
trm1p, zc376.5, ta0997, trna (m22g26)dimethyltransferase, trm1 methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tRNA (m22G26)dimethyltransferase
-
tRNA(m22G26)dimethyltransferase
-
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
additional information
?
-
-
in yeast tRNAAsp G26 is unmodified. Successive change of the near surroundings of G26 in this tRNA is performed until G26 becomes modified to N2-dimethylguanine26 tRNA by a tRNA(m2(2)G26)methyltransferase in Xenopus laevis oocytes. In this the two D-stem basepairs C1 -G24, G10-C25 are identified immediately preceding G26 as major identity elements for the dimethylating enzyme modifying G26. Increasing the extra loop in tRNAAsp from four to the more usual five bases influence the global structure of the tRNA such that the mJG26 formation is drastically decreased even if the near region of G26 had the two consensus basepairs. Not only are the two consensus base pairs in the D-stem a prerequisite for G26 modification, but also is any part of the tRNA molecule that influence the 3D-structure important for the recognition between nuclear coded tRNAs and the tRNA(mJG26)methyltransferase
-
-
?
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.2
calculated from sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
64050
calculated from sequence
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, the enzyme precipitates if stored for several days
frozen in small portions, enzyme maintains activity for at least several months
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli and the His-tagged Trm1 protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Edqvist, J.; Blomqvist, K.; Straby, K.B.
Structural elements in yeast tRNAs required for homologous modification of guanosine-26 into dimethylguanosine-26 by the yeast Trm1 tRNA-modifying enzyme
Biochemistry
33
9546-9551
1994
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Liu, J.; Zhou, G.Q.; Strabym K.B.
Caenorhabditis elegans ZC376.5 encodes a tRNA (m2/2G(26))dimethyltransferance in which (246)arginine is important for the enzyme activity
Gene
226
73-81
1999
Caenorhabditis elegans (Q23270), Caenorhabditis elegans, Saccharomyces cerevisiae (P15565), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Edqvist, J.; Grosjean, H.; Straby, K.B.
Identity elements for N2-dimethylation of guanosine-26 in yeast tRNAs
Nucleic Acids Res.
20
6575-6581
1992
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Liu, J.; Liu, J.; Straby, K.B.
Point and deletion mutations eliminate one or both methyl group transfers catalysed by the yeast TRM1 encoded tRNA (m22G26)dimethyltransferase
Nucleic Acids Res.
26
5102-5108
1998
Saccharomyces cerevisiae (P15565), Saccharomyces cerevisiae
Manually annotated by BRENDA team