BRENDA - Enzyme Database

Gln-tRNAGln formation from Glu-tRNAGln requires cooperation of an asparaginase and a Glu-tRNAGln kinase

Feng, L.; Sheppard, K.; Tumbula-Hansen, D.; Soell, D.; J. Biol. Chem. 280, 8150-8155 (2005)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
6.3.5.7
-
Methanothermobacter thermautotrophicus
Engineering
EC Number
Amino acid exchange
Commentary
Organism
6.3.5.7
D178E
glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable
Methanothermobacter thermautotrophicus
6.3.5.7
D178N
glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable
Methanothermobacter thermautotrophicus
6.3.5.7
K254E
glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable
Methanothermobacter thermautotrophicus
6.3.5.7
T101A
glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable
Methanothermobacter thermautotrophicus
6.3.5.7
T101S
hydrolyzes about 10% of glutamine compared to wild-type enzyme. Compared to wild-type enzyme, the mutant enzyme converts approximately half as much mischarged tRNA substrate to product
Methanothermobacter thermautotrophicus
6.3.5.7
T177S
mutant enzyme hydrolyzes the same amount of glutamine as the wild-type enzyme. As the wild-type enzyme, the mutant enzyme transforms most of Glu-tRNAGln to Gln-tRNAGln
Methanothermobacter thermautotrophicus
6.3.5.7
T177V
glutamine hydrolysis is negligible. Gln-tRNAGln formation is undetectable
Methanothermobacter thermautotrophicus
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
6.3.5.7
Methanothermobacter thermautotrophicus
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
6.3.5.7
-
Methanothermobacter thermautotrophicus
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6.3.5.7
ATP + Glu-tRNAGln + L-glutamine
GatDE is a heterodimeric amidotransferase. GatD acts as a glutaminase but only in the presence of both Glu-tRNAGln and the other subunit, GatE. The fact that only Glu-tRNAGln but not tRNA Gln could activate the glutaminase activity of GatD suggests that glutamine hydrolysis is coupled tightly to transamidation. GatE is a Glu-tRNAGln kinase that activates Glu-tRNAGln via gamma-phosphorylation
662450
Methanothermobacter thermautotrophicus
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
?
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
6.3.5.7
-
Methanothermobacter thermautotrophicus
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
6.3.5.7
D178E
glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable
Methanothermobacter thermautotrophicus
6.3.5.7
D178N
glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable
Methanothermobacter thermautotrophicus
6.3.5.7
K254E
glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable
Methanothermobacter thermautotrophicus
6.3.5.7
T101A
glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable
Methanothermobacter thermautotrophicus
6.3.5.7
T101S
hydrolyzes about 10% of glutamine compared to wild-type enzyme. Compared to wild-type enzyme, the mutant enzyme converts approximately half as much mischarged tRNA substrate to product
Methanothermobacter thermautotrophicus
6.3.5.7
T177S
mutant enzyme hydrolyzes the same amount of glutamine as the wild-type enzyme. As the wild-type enzyme, the mutant enzyme transforms most of Glu-tRNAGln to Gln-tRNAGln
Methanothermobacter thermautotrophicus
6.3.5.7
T177V
glutamine hydrolysis is negligible. Gln-tRNAGln formation is undetectable
Methanothermobacter thermautotrophicus
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
6.3.5.7
-
Methanothermobacter thermautotrophicus
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6.3.5.7
ATP + Glu-tRNAGln + L-glutamine
GatDE is a heterodimeric amidotransferase. GatD acts as a glutaminase but only in the presence of both Glu-tRNAGln and the other subunit, GatE. The fact that only Glu-tRNAGln but not tRNA Gln could activate the glutaminase activity of GatD suggests that glutamine hydrolysis is coupled tightly to transamidation. GatE is a Glu-tRNAGln kinase that activates Glu-tRNAGln via gamma-phosphorylation
662450
Methanothermobacter thermautotrophicus
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
?