Information on EC 2.1.1.221 - tRNA (guanine9-N1)-methyltransferase

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
2.1.1.221
-
RECOMMENDED NAME
GeneOntology No.
tRNA (guanine9-N1)-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + guanine9 in tRNA = S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (guanine9-N1)-methyltransferase
The enzyme from Saccharomyces cerevisiae specifically methylates guanine9 [1,2]. The bifunctional enzyme from Thermococcus kodakaraensis also catalyses the methylation of adenine9 in tRNA (cf. EC 2.1.1.218, tRNA (adenine9-N1)-methyltransferase) [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
show the reaction diagram
S-adenosyl-L-methionine + guanine9 in tRNACysGCA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNACysGCA
show the reaction diagram
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
show the reaction diagram
S-adenosyl-L-methionine + guanine9 in tRNAGlyCCC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGlyCCC
show the reaction diagram
S-adenosyl-L-methionine + guanine9 in tRNAGlyGCC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGlyGCC
show the reaction diagram
S-adenosyl-L-methionine + guanine9 in tRNALeuCAA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNALeuCAA
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNALeuGAG
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNALeuGAG
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNALysCUU
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNALysCUU
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAThrAGU
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAThrAGU
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAThrCGU
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAThrCGU
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAValUAC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAValUAC
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
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
show the reaction diagram
S-adenosyl-L-methionine + guanine9 in tRNACysGCA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNACysGCA
show the reaction diagram
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
show the reaction diagram
S-adenosyl-L-methionine + guanine9 in tRNAGlyCCC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGlyCCC
show the reaction diagram
S-adenosyl-L-methionine + guanine9 in tRNAGlyGCC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGlyGCC
show the reaction diagram
S-adenosyl-L-methionine + guanine9 in tRNALeuCAA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNALeuCAA
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNALeuGAG
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNALeuGAG
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNALysCUU
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNALysCUU
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAThrAGU
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAThrAGU
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAThrCGU
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAThrCGU
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAValUAC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAValUAC
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
SDR5C1 protein
enzyme TrmT10C requires another protein, SDR5C1 (MRPP2), to execute its m1R9 (G9 and A9) MTase and additional RNase P activity
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0032 - 0.0053
guanine9 in tRNAGly
-
0.00016 - 0.0024
guanine9 in tRNAGlyGCC
-
0.00023 - 0.00186
guanine9 in tRNAValUAC
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0027 - 0.0028
guanine9 in tRNAGly
-
0.0023 - 0.009
guanine9 in tRNAGlyGCC
-
0.0052 - 0.012
guanine9 in tRNAValUAC
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.538 - 1.66
guanine9 in tRNAGly
210522
3.75 - 75
guanine9 in tRNAGlyGCC
210523
2.8 - 52.17
guanine9 in tRNAValUAC
210524
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9.75
the bifunctional enzyme is active in a pH range 5.5-9.75. The intensity of m1A and m1G spots varies greatly as a function of the pH. At pH 5.5, m1A MTase activity of TK0422p is predominant over m1G. At pH 7 or higher, both m1A and m1G are detected, m1G intensity growing with increasing pH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
TRMT10A is expressed in human embryonic and fetal brain, TRMT10A expression profile in fetal telencephalon, overview
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
TRMT10A has predominant nuclear localization. TRMT10A localizes to the nucleolus of beta- and non-beta-cells, where tRNA modifications occur
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified enzyme in complex with S-adenosyl-L-homocysteine, X-ray diffraction structure determination and analysis at 1.8 A resolution, molecular replacement
-
purified enzyme free or in complex with S-adenosyl-L-homocysteine, X-ray diffraction structure determination and analysis at 2.0-2.5 A resolution, molecular replacement
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
-
recombinant N-terminally His-tagged enzyme Trm10 from Escherichia coli strain BL21/Gold(DE3) by nickel affinity chromatography, gel filtration, and anion exchange chromatography, followed by dialysis
-
recombinant N-terminally His-tagged enzyme Trm10 from Escherichia coli strain BL21/Gold(DE3) by nickel affinity chromatography, gel filtration, and anion exchange chromatography, followed by dialysis. Purification of the recombinant TrmT10C-SDR5C1 wild-type and mutant complexes by nickel affinity chromatography
recombinant N-terminally His6-tagged enzyme from Escherichia coli by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene trm10, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli
gene TRMT10A or RG9MTD2, genotyping
overexpression in Escherichia coli
-
recombinant expression of N-terminally His-tagged enzyme Trm10 in Escherichia coli strain BL21/Gold(DE3)
-
recombinant expression of N-terminally His-tagged enzyme Trm10 in Escherichia coli strain BL21/Gold(DE3), selenomethionine-labeled spTrm10_74 (residues 74-281) is expressed in Escherichia coli strain B834, recombinant wild-type and mutant Q226A TrmT10C (residues 40-403) is coexpressed with His-tagged protein SDR5C1
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R127stop
naturally occuring nonsene mutation involved in the syndrome of young onset diabetes
D210N
-
site-directed mutagenesis, inactive mutant
N212A
-
site-directed mutagenesis, the mutant shows increased Km for tRNA compared to the wild-type
D210N
-
site-directed mutagenesis, inactive mutant
-
N212A
-
site-directed mutagenesis, the mutant shows increased Km for tRNA compared to the wild-type
-
D207N
site-directed mutagenesis, inactive mutant
K110E/R121E/R127E
site-directed mutagenesis, inactive mutant
K153E/R147E
site-directed mutagenesis, inactive mutant
K208A
site-directed mutagenesis, mutation of a nucleoside binding pocket residue, the mutant shows 28% reduced activity compared to the wild-type enzyme
N209A
site-directed mutagenesis, the mutant shows increased Km for tRNA compared to the wild-type
Q118A
site-directed mutagenesis, mutation of a nucleoside binding pocket residue, inactive mutant
T244A
site-directed mutagenesis, mutation of a nucleoside binding pocket residue, the mutant shows 65% reduced activity compared to the wild-type enzyme
V206A
site-directed mutagenesis, mutation of a nucleoside binding pocket residue, the mutant shows 81% reduced activity compared to the wild-type enzyme
D207N
-
site-directed mutagenesis, inactive mutant
-
K208A
-
site-directed mutagenesis, mutation of a nucleoside binding pocket residue, the mutant shows 28% reduced activity compared to the wild-type enzyme
-
N209A
-
site-directed mutagenesis, the mutant shows increased Km for tRNA compared to the wild-type
-
Q118A
-
site-directed mutagenesis, mutation of a nucleoside binding pocket residue, inactive mutant
-
T244A
-
site-directed mutagenesis, mutation of a nucleoside binding pocket residue, the mutant shows 65% reduced activity compared to the wild-type enzyme
-