BRENDA - Enzyme Database show
show all sequences of 6.3.5.7

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)
Commentary
Organism
-
Methanothermobacter thermautotrophicus
Engineering
Amino acid exchange
Commentary
Organism
D178E
glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable
Methanothermobacter thermautotrophicus
D178N
glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable
Methanothermobacter thermautotrophicus
K254E
glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable
Methanothermobacter thermautotrophicus
T101A
glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable
Methanothermobacter thermautotrophicus
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
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
T177V
glutamine hydrolysis is negligible. Gln-tRNAGln formation is undetectable
Methanothermobacter thermautotrophicus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanothermobacter thermautotrophicus
-
-
-
Purification (Commentary)
Commentary
Organism
-
Methanothermobacter thermautotrophicus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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)
Commentary
Organism
-
Methanothermobacter thermautotrophicus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D178E
glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable
Methanothermobacter thermautotrophicus
D178N
glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable
Methanothermobacter thermautotrophicus
K254E
glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable
Methanothermobacter thermautotrophicus
T101A
glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable
Methanothermobacter thermautotrophicus
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
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
T177V
glutamine hydrolysis is negligible. Gln-tRNAGln formation is undetectable
Methanothermobacter thermautotrophicus
Purification (Commentary) (protein specific)
Commentary
Organism
-
Methanothermobacter thermautotrophicus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
-
-
-
?
Other publictions for EC 6.3.5.7
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)
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728391
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Gln-tRNAGln synthesis in a dyn ...
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Nucleic Acids Res.
39
9306-9315
2011
1
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1
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728668
O'Donoghue
Rational design of an evolutio ...
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Proc. Natl. Acad. Sci. USA
108
20485-20490
2011
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1
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4
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1
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4
4
709508
Chatani
A simple turbidimetric method ...
Staphylococcus aureus
J. Microbiol. Methods
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2010
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714451
Balg
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Bioorg. Med. Chem.
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7
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4
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Nature
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716371
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Methanothermobacter thermautotrophicus
Nucleic Acids Res.
38
5774-5783
2010
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3
3
706514
Nagao
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106
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2009
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692759
Balg
Inhibition of Helicobacter pyl ...
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J. Am. Chem. Soc.
130
3264-3265
2008
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8
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673689
Namgoong
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FEBS Lett.
581
309-314
2007
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674787
Sheppard
The Helicobacter pylori amidot ...
Helicobacter pylori
J. Biol. Chem.
282
11866-11873
2007
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3
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662450
Feng
Gln-tRNAGln formation from Glu ...
Methanothermobacter thermautotrophicus
J. Biol. Chem.
280
8150-8155
2005
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7
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492304
Harpel
Mutagenesis and mechanism-base ...
Streptococcus pyogenes
Biochemistry
41
6398-6407
2002
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492305
Kwak
Expression, purification, and ...
Geobacillus stearothermophilus
Mol. Cells
14
374-381
2002
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1
1
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492302
Horiuchi
Mechanistic studies of reactio ...
Streptococcus pyogenes
Biochemistry
40
6450-6457
2001
1
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3
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492308
Salazar
A dual-specific Glu-tRNA(Gln) ...
Acidithiobacillus ferrooxidans
FEBS Lett.
500
129-131
2001
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1
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492303
Curnow
Glu-tRNAGln amidotransferase: ...
Bacillus subtilis
Proc. Natl. Acad. Sci. USA
94
11819-11826
1997
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1
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3
1
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5
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1
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1
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1
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-
492291
Vothknecht
-
Charging of both, plastidial t ...
Tetradesmus obliquus
Z. Naturforsch. C
50
789-795
1995
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1
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