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show all sequences of 2.1.1.B43

Archease from Pyrococcus abyssi improves substrate specificity and solubility of a tRNA m5C methyltransferase

Auxilien, S.; El Khadali, F.; Rasmussen, A.; Douthwaite, S.; Grosjean, H.; J. Biol. Chem. 282, 18711-18721 (2007)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
archaease
in vitro, the purified recombinant methyltransferase catalyzes 5-methylcytosine formation at several cytosines within tRNAs with preference for C49. The specificity of the methyltransferase is increased by the archease. In solution, the archease exists as a monomer, trimer, and hexamer. Only the oligomeric states bind the methyltransferase and prevent its aggregation, in addition to hindering dimerization of the methyltransferase-tRNA complex
Pyrococcus abyssi
Cloned(Commentary)
Commentary
Organism
-
Pyrococcus abyssi
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35747
-
x * 35747, calculated from sequence
Pyrococcus abyssi
35750
-
calculated from sequence
Pyrococcus abyssi
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pyrococcus abyssi
Q9V106
-
-
Purification (Commentary)
Commentary
Organism
-
Pyrococcus abyssi
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
S-adenosyl-L-methionine + cytosine49 in tRNA
tRNAASp. In vitro, the purified recombinant methyltransferase catalyzes 5-methylcytosine formation at several cytosines within tRNAs with preference for C49. When tRNA is incubated with the PAB1947 enzyme at 50C instead of 80C, methylation becomes more specific for the 4751 sequence. Addition of archease to the methylation reactions with Pyrococcus abyssi tRNAAsp at 80C increases modification within the oligonucleotide ACCCG that contains cytidine49, while reducing modification at unspecific sites. The unstructured poly(C)RNA is effectively methylated at 50C, with most of the tritiated label from the methyl donor becoming incorporated into the RNA. However, when the recombinant PAB1947 enzyme is substituted with a Pyrococcus abyssi cell extract, no methylation of the poly(C) RNA occurs
708990
Pyrococcus abyssi
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 35747, calculated from sequence
Pyrococcus abyssi
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
archaease
in vitro, the purified recombinant methyltransferase catalyzes 5-methylcytosine formation at several cytosines within tRNAs with preference for C49. The specificity of the methyltransferase is increased by the archease. In solution, the archease exists as a monomer, trimer, and hexamer. Only the oligomeric states bind the methyltransferase and prevent its aggregation, in addition to hindering dimerization of the methyltransferase-tRNA complex
Pyrococcus abyssi
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Pyrococcus abyssi
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35747
-
x * 35747, calculated from sequence
Pyrococcus abyssi
35750
-
calculated from sequence
Pyrococcus abyssi
Purification (Commentary) (protein specific)
Commentary
Organism
-
Pyrococcus abyssi
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
S-adenosyl-L-methionine + cytosine49 in tRNA
tRNAASp. In vitro, the purified recombinant methyltransferase catalyzes 5-methylcytosine formation at several cytosines within tRNAs with preference for C49. When tRNA is incubated with the PAB1947 enzyme at 50C instead of 80C, methylation becomes more specific for the 4751 sequence. Addition of archease to the methylation reactions with Pyrococcus abyssi tRNAAsp at 80C increases modification within the oligonucleotide ACCCG that contains cytidine49, while reducing modification at unspecific sites. The unstructured poly(C)RNA is effectively methylated at 50C, with most of the tritiated label from the methyl donor becoming incorporated into the RNA. However, when the recombinant PAB1947 enzyme is substituted with a Pyrococcus abyssi cell extract, no methylation of the poly(C) RNA occurs
708990
Pyrococcus abyssi
S-adenosyl-L-homocysteine + 5-methylcytosine49 in tRNA
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 35747, calculated from sequence
Pyrococcus abyssi
Other publictions for EC 2.1.1.B43
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
708990
Auxilien
Archease from Pyrococcus abyss ...
Pyrococcus abyssi
J. Biol. Chem.
282
18711-18721
2007
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