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Enzyme Nomenclature
Information on EC 2.1.1.221 - tRNA (guanine9-N1)-methyltransferase
for references in articles please use BRENDA:EC2.1.1.221
Word Map on EC 2.1.1.221
- 2.1.1.221
- archaea
- microcephaly
-
methyltransferases
-
spout
-
disabl
-
intellectual
- disability
-
nonsense
- children
- mellitus
-
exome
-
siblings
-
stature
- islet
- guanosine
- trnagly
-
circumference
- puberty
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The expected taxonomic range for this enzyme is: Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
2.1.1.221
-
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RECOMMENDED NAME
GeneOntology No.
tRNA (guanine9-N1)-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + guanine9 in tRNA = S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
S-adenosyl-L-methionine + guanine9 in tRNA = S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
-
S-adenosyl-L-methionine + guanine9 in tRNA = S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
catalytic mechanism and recognition of tRNA substrate, overview. The N-terminal extension of Trm10 is necessary for substrate tRNA recognition
-
S-adenosyl-L-methionine + guanine9 in tRNA = S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
catalytic mechanism and recognition of tRNA substrate, overview. The N-terminal extension of Trm10 is necessary for substrate tRNA recognition
S-adenosyl-L-methionine + guanine9 in tRNA = S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
catalytic mechanism and recognition of tRNA substrate, overview. The N-terminal extension of Trm10 is necessary for substrate tRNA recognition
-
-
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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].
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
additional information
evolution
-
the enzyme Trm10 belongs to the SPOUT superfamily. Trm10 behaves as a monomer in solution, whereas other members of the SPOUT superfamily all function as homodimers. The MTase domain (the catalytic domain) of the Trm10 family displays a typical SpoU-TrmD (SPOUT) fold. Trm10 from Schizosaccharomyces pombe demonstrates identical tRNA MTase activity as Trm10 from Saccharomyces cerevisiae
evolution
the enzyme Trm10 belongs to the SPOUT superfamily. Trm10 behaves as a monomer in solution, whereas other members of the SPOUT superfamily all function as homodimers. The MTase domain (the catalytic domain) of the Trm10 family displays a typical SpoU-TrmD (SPOUT) fold. Trm10 from Schizosaccharomyces pombe demonstrates identical tRNA MTase activity as Trm10 from Saccharomyces cerevisiae
evolution
N-1 methylation of the nearly invariant purine residue found at position 9 of tRNA is a nucleotide modification found in multiple tRNA species throughout Eukarya and Archaea
evolution
-
N-1 methylation of the nearly invariant purine residue found at position 9 of tRNA is a nucleotide modification found in multiple tRNA species throughout Eukarya and Archaea. The tRNA methyltransferase Trm10 is a highly conserved protein both necessary and sufficient to catalyze all known instances of m1G9 modification in yeast
evolution
-
the enzyme Trm10 belongs to the SPOUT superfamily. Trm10 behaves as a monomer in solution, whereas other members of the SPOUT superfamily all function as homodimers. The MTase domain (the catalytic domain) of the Trm10 family displays a typical SpoU-TrmD (SPOUT) fold. Trm10 from Schizosaccharomyces pombe demonstrates identical tRNA MTase activity as Trm10 from Saccharomyces cerevisiae
-
malfunction
-
guanine9 methylation activity is not detectable in trm10-DELTA/trm10-DELTA strain
malfunction
TRMT10A silencing induces human beta-cell apoptosis.. TRMT10A deficiency negatively affects beta-cell mass and the pool of neurons in the developing brain. A nonsense mutation R127stop in the enzyme is involved in the syndrome of young onset diabetes, short stature and microcephaly (small brain size) with intellectual disability in a large consanguineous family, TRMT10A mRNA and protein are absent in cells from affected siblings, phenotype, overview. Patients are homozygous for a nonsense mutation in TRMT10A and lose TRMT10A expression
additional information
-
enzyme overall structure analysis, active site structure, overview
additional information
enzyme overall structure analysis, active site structure, overview
additional information
-
enzyme overall structure analysis, active site structure, overview
additional information
-
enzyme overall structure analysis, active site structure, overview
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
S-adenosyl-L-methionine + guanine9 in tRNACysGCA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNACysGCA
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
S-adenosyl-L-methionine + guanine9 in tRNAGlyCCC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGlyCCC
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAGlyGCC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGlyGCC
S-adenosyl-L-methionine + guanine9 in tRNALeuCAA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNALeuCAA
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNALeuGAG
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNALeuGAG
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNALysCUU
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNALysCUU
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAThrAGU
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAThrAGU
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAThrCGU
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAThrCGU
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAValUAC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAValUAC
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
TRM10 is required for the catalysis of at least 9 of the 10 m1G modifications observed (tRNA(Trp), tRNA(Pro), tRNA(Val), tRNAi(Met), tRNA(Ile), tRNAICG(Arg), and both tRNAUCU(Arg) species) at position 9 in yeast. It is likely that Trm10p is also responsible for modification of G9 of tRNAAla
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
the enzyme is specific for guanine9 in tRNA, does not catalyse methylation of adenine9 in tRNA
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
the bifunctional enzyme catalyzes both methylation of guanine9 and methylation of adenine9 in tRNA
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
formation of N1-methylguanine9 in tRNA(Asp) from Thermococcus kodakaraensis that contains a guanosine at position 9. The enzyme forms approximately the same amount of m1A and m1G when the tRNA of the yeast strain Y16243 is used as substrate. Given that occurrence of A9 and G9 in this tRNA population is almost equal (about 50% each) this result indicates that the enzyme TK0422p does not show any preference for one of these two nucleosides. The ratio m1A/m1G formed from Escherichia coli tRNA is higher than that with tRNA from the yeast Y16243 strain. This is consistent with the fact that there are about two times more tRNAs with A9 than with G9 in Escherichia coli. The 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
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
-
Trm10 is specific for G9 of tRNAGly
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
Trm10 is specific for G9 of tRNAGly
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
Trm10 is specific for G9 of tRNAGly
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAGlyGCC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGlyGCC
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAGlyGCC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGlyGCC
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAValUAC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAValUAC
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAValUAC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAValUAC
-
-
-
-
?
additional information
?
-
substrate specificity analysis in vivo, overview
-
-
-
additional information
?
-
-
there are 19 unique tRNA species that contain a G at position 9 in yeast, and whose fully modified sequence is known, only 9 of these tRNA species are modified with m1G9 in wild-type cells. The in vitro methylation activity of yeast Trm10 is not sufficient to explain the observed pattern of modification in vivo, as additional tRNA species are substrates for Trm10 m1G9 methyltransferase activity, substrate specificity analysis in vivo, overview
-
-
-
additional information
?
-
-
no activity of the enzyme with three sptRNAGly mutants at Position 9 (G9A, G9C, and G9U)
-
-
-
additional information
?
-
no activity of the enzyme with three sptRNAGly mutants at Position 9 (G9A, G9C, and G9U)
-
-
-
additional information
?
-
-
no activity of the enzyme with three sptRNAGly mutants at Position 9 (G9A, G9C, and G9U)
-
-
-
additional information
?
-
no activity of the enzyme with three sptRNAGly mutants at Position 9 (G9A, G9C, and G9U)
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
S-adenosyl-L-methionine + guanine9 in tRNACysGCA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNACysGCA
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
S-adenosyl-L-methionine + guanine9 in tRNAGlyCCC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGlyCCC
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAGlyGCC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGlyGCC
S-adenosyl-L-methionine + guanine9 in tRNALeuCAA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNALeuCAA
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNALeuGAG
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNALeuGAG
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNALysCUU
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNALysCUU
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAThrAGU
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAThrAGU
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAThrCGU
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAThrCGU
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAValUAC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAValUAC
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
Q8TBZ6
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
Q12400
TRM10 is required for the catalysis of at least 9 of the 10 m1G modifications observed (tRNA(Trp), tRNA(Pro), tRNA(Val), tRNAi(Met), tRNA(Ile), tRNAICG(Arg), and both tRNAUCU(Arg) species) at position 9 in yeast. It is likely that Trm10p is also responsible for modification of G9 of tRNAAla
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNA
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNA
Q5JD38
the bifunctional enzyme catalyzes both methylation of guanine9 and methylation of adenine9 in tRNA
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
-
Trm10 is specific for G9 of tRNAGly
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
O14214
Trm10 is specific for G9 of tRNAGly
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAGly
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGly
O14214
Trm10 is specific for G9 of tRNAGly
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAGlyGCC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGlyGCC
Q8TBZ6
-
-
-
?
S-adenosyl-L-methionine + guanine9 in tRNAGlyGCC
S-adenosyl-L-homocysteine + N1-methylguanine9 in tRNAGlyGCC
-
-
-
-
?
additional information
?
-
Q8TBZ6
substrate specificity analysis in vivo, overview
-
-
-
additional information
?
-
-
there are 19 unique tRNA species that contain a G at position 9 in yeast, and whose fully modified sequence is known, only 9 of these tRNA species are modified with m1G9 in wild-type cells. The in vitro methylation activity of yeast Trm10 is not sufficient to explain the observed pattern of modification in vivo, as additional tRNA species are substrates for Trm10 m1G9 methyltransferase activity, substrate specificity analysis in vivo, overview
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SDR5C1 protein
enzyme TrmT10C requires another protein, SDR5C1 (MRPP2), to execute its m1R9 (G9 and A9) MTase and additional RNase P activity
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0032
guanine9 in tRNAGly
tRNA from Schizosaccharomyces pombe, recombinant enzyme, pH and temperature not specified in the publication
-
0.0053
guanine9 in tRNAGly
-
tRNA from Schizosaccharomyces pombe, recombinant enzyme, pH and temperature not specified in the publication
-
additional information
additional information
-
kinetic mechanism of Trm10, overview
-
additional information
additional information
kinetic mechanism of Trm10, overview
-
additional information
additional information
-
kinetic mechanism of Trm10, overview
-
additional information
additional information
steady-state kinetics, overview
-
additional information
additional information
-
steady-state kinetics, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0027
guanine9 in tRNAGly
tRNA from Schizosaccharomyces pombe, recombinant enzyme, pH and temperature not specified in the publication
-
0.0028
guanine9 in tRNAGly
-
tRNA from Schizosaccharomyces pombe, recombinant enzyme, pH and temperature not specified in the publication
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.538
guanine9 in tRNAGly
-
tRNA from Schizosaccharomyces pombe, recombinant enzyme, pH and temperature not specified in the publication
-
1.66
guanine9 in tRNAGly
tRNA from Schizosaccharomyces pombe, recombinant enzyme, pH and temperature not specified in the publication
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
TRMT10A is expressed in human embryonic and fetal brain, TRMT10A expression profile in fetal telencephalon, overview
additional information
additional information
-
TRMT10A is ubiquitously expressed but enriched in brain and pancreatic islets
additional information
TRMT10A is ubiquitously expressed but enriched in brain and pancreatic islets
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
TRMT10A has predominant nuclear localization. TRMT10A localizes to the nucleolus of beta- and non-beta-cells, where tRNA modifications occur
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Q12400
Saccharomyces cerevisiae (strain ATCC 204508 / S288c);
Schizosaccharomyces pombe (strain 972 / ATCC 24843);
O14214
Schizosaccharomyces pombe (strain 972 / ATCC 24843);
O14214
Schizosaccharomyces pombe (strain 972 / ATCC 24843);
O14214
Schizosaccharomyces pombe (strain 972 / ATCC 24843);
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
-
the enzyme adopts a globular alpha/beta structure consisting of six-stranded beta-sheets sandwiched by alpha-helices at both sides, small angle X-ray scattering analysis
monomer
the enzyme adopts a globular alpha/beta structure consisting of six-stranded beta-sheets sandwiched by alpha-helices at both sides, small angle X-ray scattering analysis
monomer
-
the enzyme adopts a globular alpha/beta structure consisting of six-stranded beta-sheets sandwiched by alpha-helices at both sides, small angle X-ray scattering analysis
-
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
recombinant N-terminally His6-tagged enzyme from Escherichia coli by nickel affinity chromatography
recombinant N-terminally His6-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene trm10, recombinant expression of N-terminally His6-tagged enzyme 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
gene trm10, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli
gene trm10, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R127stop
naturally occuring nonsene mutation involved in the syndrome of young onset diabetes
N212A
-
site-directed mutagenesis, the mutant shows increased Km for tRNA compared to the wild-type
K110E/R121E/R127E
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
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
-
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LINKS TO OTHER DATABASES (specific for EC-Number 2.1.1.221)
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