BRENDA - Enzyme Database

Major identity element of glutamine tRNAs from Bacillus subtilis and Escherichia coli in the reaction with B. subtilis glutamyl-tRNA synthetase

Kim, S.I.; Soll, D.; Mol. Cells 8, 459-465 (1998)

Data extracted from this reference:

Engineering
EC Number
Amino acid exchange
Commentary
Organism
6.1.1.17
additional information
construction and expression in Escherichia coli of mutant forms of Escherichia coli tRNAGln2 and tRNAGln1 and of Bacillus subtilis tRNAGln
Bacillus subtilis
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
6.1.1.17
ATP + L-glutamate + tRNAGlu
Bacillus subtilis
-
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Bacillus subtilis
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
6.1.1.17
Bacillus subtilis
-
-
-
6.1.1.24
Bacillus subtilis
-
-
-
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
6.1.1.17
additional information
-
glutamate and glutamine acceptor activity with wild-type and mutant tRNAGlns with native and recombinant enzyme, overview
Bacillus subtilis
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6.1.1.17
ATP + L-glutamate + tRNAGln
enzyme is active with the tRNAGln from Bacillus subtilis and the isoacceptor tRNAGln1, but not tRNAGln2, from Escherichia coli, the major recognition element is U at position 34
492290
Bacillus subtilis
AMP + diphosphate + L-glutamyl-tRNAGln
-
492290
Bacillus subtilis
?
6.1.1.17
ATP + L-glutamate + tRNAGlu
-
492290
Bacillus subtilis
AMP + diphosphate + L-glutamyl-tRNAGlu
-
492290
Bacillus subtilis
?
6.1.1.17
ATP + L-glutamate + tRNAGlu
enzyme utilizes tRNAGlu from Bacillus subtilis, not from Escherichia coli
492290
Bacillus subtilis
AMP + diphosphate + L-glutamyl-tRNAGlu
-
492290
Bacillus subtilis
?
6.1.1.17
additional information
glutamate and glutamine acceptor activity with wild-type and mutant tRNAGlns with native and recombinant enzyme, overview
492290
Bacillus subtilis
?
-
492290
Bacillus subtilis
?
6.1.1.24
ATP + L-glutamate + tRNAGln
-
492290
Bacillus subtilis
AMP + diphosphate + Glu-tRNAGln
-
492290
Bacillus subtilis
?
6.1.1.24
ATP + L-glutamate + tRNAGlu
major recognition element for the enzyme is U at the 34th position of both tRNA1Gln from Bacillus subtilis and tRNA1Gln from E. coli as a modified form
492290
Bacillus subtilis
AMP + diphosphate + Glu-tRNAGlu
-
492290
Bacillus subtilis
?
Temperature Optimum [░C]
EC Number
Temperature Optimum [░C]
Temperature Optimum Maximum [░C]
Commentary
Organism
6.1.1.17
37
-
assay at
Bacillus subtilis
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.1.1.17
7
-
assay at
Bacillus subtilis
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
6.1.1.17
ATP
-
Bacillus subtilis
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
6.1.1.17
ATP
-
Bacillus subtilis
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
6.1.1.17
additional information
construction and expression in Escherichia coli of mutant forms of Escherichia coli tRNAGln2 and tRNAGln1 and of Bacillus subtilis tRNAGln
Bacillus subtilis
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
6.1.1.17
ATP + L-glutamate + tRNAGlu
Bacillus subtilis
-
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Bacillus subtilis
?
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
6.1.1.17
additional information
-
glutamate and glutamine acceptor activity with wild-type and mutant tRNAGlns with native and recombinant enzyme, overview
Bacillus subtilis
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6.1.1.17
ATP + L-glutamate + tRNAGln
enzyme is active with the tRNAGln from Bacillus subtilis and the isoacceptor tRNAGln1, but not tRNAGln2, from Escherichia coli, the major recognition element is U at position 34
492290
Bacillus subtilis
AMP + diphosphate + L-glutamyl-tRNAGln
-
492290
Bacillus subtilis
?
6.1.1.17
ATP + L-glutamate + tRNAGlu
-
492290
Bacillus subtilis
AMP + diphosphate + L-glutamyl-tRNAGlu
-
492290
Bacillus subtilis
?
6.1.1.17
ATP + L-glutamate + tRNAGlu
enzyme utilizes tRNAGlu from Bacillus subtilis, not from Escherichia coli
492290
Bacillus subtilis
AMP + diphosphate + L-glutamyl-tRNAGlu
-
492290
Bacillus subtilis
?
6.1.1.17
additional information
glutamate and glutamine acceptor activity with wild-type and mutant tRNAGlns with native and recombinant enzyme, overview
492290
Bacillus subtilis
?
-
492290
Bacillus subtilis
?
6.1.1.24
ATP + L-glutamate + tRNAGln
-
492290
Bacillus subtilis
AMP + diphosphate + Glu-tRNAGln
-
492290
Bacillus subtilis
?
6.1.1.24
ATP + L-glutamate + tRNAGlu
major recognition element for the enzyme is U at the 34th position of both tRNA1Gln from Bacillus subtilis and tRNA1Gln from E. coli as a modified form
492290
Bacillus subtilis
AMP + diphosphate + Glu-tRNAGlu
-
492290
Bacillus subtilis
?
Temperature Optimum [░C] (protein specific)
EC Number
Temperature Optimum [░C]
Temperature Optimum Maximum [░C]
Commentary
Organism
6.1.1.17
37
-
assay at
Bacillus subtilis
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.1.1.17
7
-
assay at
Bacillus subtilis