BRENDA - Enzyme Database show
show all sequences of 6.3.5.7

Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation

Curnow, A.W.; Hong, K.W.; Yuan, R.; Kim, S.I.; Martins, O.; Winkler, W.; Henkin, T.M.; Soll, D.; Proc. Natl. Acad. Sci. USA 94, 11819-11826 (1997)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
cloning of the three genes, gatC, gatA, and gatB, which constitute the transcriptional unit of the enzyme
Bacillus subtilis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Bacillus subtilis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
10900
-
1 * 53000 + 1 * 53500 + 1 * 10900, SDS-PAGE
Bacillus subtilis
53000
-
1 * 53000 + 1 * 53500 + 1 * 10900, SDS-PAGE
Bacillus subtilis
53500
-
1 * 53000 + 1 * 53500 + 1 * 10900, SDS-PAGE
Bacillus subtilis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + Glu-tRNAGln + L-glutamine
Bacillus subtilis
disruption of this operon is lethal. Transamidation is the only pathway to Gln-tRNAGln in Bacillus subtilis. The enzyme furnishes a means for formation of correctly charged Gln-tRNAGln through the transamidation of misacylated Glu-tRNAGln, functionally replacing the lack of glutaminyl-tRNA synthetase activity in Gram-positive eubacteria, cyanobacteria, archaea and organelles
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus subtilis
-
-
-
Purification (Commentary)
Commentary
Organism
-
Bacillus subtilis
Specific Activity [micromol/min/mg]
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
0.009
-
-
Bacillus subtilis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + Glu-tRNAGln + Asn
Asn is much less effective as amide donor than glutamine
492303
Bacillus subtilis
ADP + phosphate + Gln-tRNAGln + Asp
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine
-
492303
Bacillus subtilis
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
492303
Bacillus subtilis
?
ATP + Glu-tRNAGln + L-glutamine
disruption of this operon is lethal. Transamidation is the only pathway to Gln-tRNAGln in Bacillus subtilis. The enzyme furnishes a means for formation of correctly charged Gln-tRNAGln through the transamidation of misacylated Glu-tRNAGln, functionally replacing the lack of glutaminyl-tRNA synthetase activity in Gram-positive eubacteria, cyanobacteria, archaea and organelles
492303
Bacillus subtilis
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
?
ATP + Glu-tRNAGln + NH4Cl
NH4Cl is much less effective as amide donor than glutamine
492303
Bacillus subtilis
ADP + phosphate + Gln-tRNAGln + ?
-
-
-
?
Subunits
Subunits
Commentary
Organism
trimer
1 * 53000 + 1 * 53500 + 1 * 10900, SDS-PAGE
Bacillus subtilis
Cloned(Commentary) (protein specific)
Commentary
Organism
cloning of the three genes, gatC, gatA, and gatB, which constitute the transcriptional unit of the enzyme
Bacillus subtilis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Bacillus subtilis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
10900
-
1 * 53000 + 1 * 53500 + 1 * 10900, SDS-PAGE
Bacillus subtilis
53000
-
1 * 53000 + 1 * 53500 + 1 * 10900, SDS-PAGE
Bacillus subtilis
53500
-
1 * 53000 + 1 * 53500 + 1 * 10900, SDS-PAGE
Bacillus subtilis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + Glu-tRNAGln + L-glutamine
Bacillus subtilis
disruption of this operon is lethal. Transamidation is the only pathway to Gln-tRNAGln in Bacillus subtilis. The enzyme furnishes a means for formation of correctly charged Gln-tRNAGln through the transamidation of misacylated Glu-tRNAGln, functionally replacing the lack of glutaminyl-tRNA synthetase activity in Gram-positive eubacteria, cyanobacteria, archaea and organelles
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Bacillus subtilis
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
0.009
-
-
Bacillus subtilis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + Glu-tRNAGln + Asn
Asn is much less effective as amide donor than glutamine
492303
Bacillus subtilis
ADP + phosphate + Gln-tRNAGln + Asp
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine
-
492303
Bacillus subtilis
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
492303
Bacillus subtilis
?
ATP + Glu-tRNAGln + L-glutamine
disruption of this operon is lethal. Transamidation is the only pathway to Gln-tRNAGln in Bacillus subtilis. The enzyme furnishes a means for formation of correctly charged Gln-tRNAGln through the transamidation of misacylated Glu-tRNAGln, functionally replacing the lack of glutaminyl-tRNA synthetase activity in Gram-positive eubacteria, cyanobacteria, archaea and organelles
492303
Bacillus subtilis
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
?
ATP + Glu-tRNAGln + NH4Cl
NH4Cl is much less effective as amide donor than glutamine
492303
Bacillus subtilis
ADP + phosphate + Gln-tRNAGln + ?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
trimer
1 * 53000 + 1 * 53500 + 1 * 10900, SDS-PAGE
Bacillus subtilis
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)
745335
Mailu
Plasmodium apicoplast Gln-tRN ...
Plasmodium berghei, Plasmodium berghei ANKA, Plasmodium falciparum
J. Biol. Chem.
290
29629-29641
2015
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6
1
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1
1
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745612
Dewage
Computational analysis of amm ...
Staphylococcus aureus, Staphylococcus aureus ATCC 700699
J. Phys. Chem. B
119
3669-3677
2015
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1
4
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2
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743955
Chongdar
Preliminary X-ray crystallogr ...
Escherichia coli
Acta Crystallogr. Sect. F
70
922-927
2014
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1
1
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1
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744268
Echevarria
Glutamyl-tRNAGln amidotransfe ...
Mus musculus
Biochem. J.
460
91-101
2014
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1
1
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745552
Hadd
Coevolution of specificity de ...
Saccharomyces cerevisiae
J. Mol. Biol.
426
3619-3633
2014
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1
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4
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1
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2
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2
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1
1
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2
2
728154
Grant
The structure of yeast glutami ...
Thermotoga maritima
J. Mol. Biol.
425
2480-2493
2013
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728391
Huot
Gln-tRNAGln synthesis in a dyn ...
Helicobacter pylori
Nucleic Acids Res.
39
9306-9315
2011
1
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3
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1
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1
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2
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728668
O'Donoghue
Rational design of an evolutio ...
Methanothermobacter thermautotrophicus
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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1
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1
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4
4
709508
Chatani
A simple turbidimetric method ...
Staphylococcus aureus
J. Microbiol. Methods
80
117-122
2010
-
1
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714451
Balg
Inhibition of Helicobacter pyl ...
Helicobacter pylori
Bioorg. Med. Chem.
18
7868-7872
2010
-
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7
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4
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1
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7
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7
7
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1
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1
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716331
Ito
Two enzymes bound to one trans ...
Thermotoga maritima
Nature
467
612-616
2010
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1
1
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716371
Rampias
The archaeal transamidosome fo ...
Methanothermobacter thermautotrophicus
Nucleic Acids Res.
38
5774-5783
2010
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1
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3
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2
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3
3
706514
Nagao
Biogenesis of glutaminyl-mt tR ...
Homo sapiens
Proc. Natl. Acad. Sci. USA
106
16209-16214
2009
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3
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692759
Balg
Inhibition of Helicobacter pyl ...
Helicobacter pylori
J. Am. Chem. Soc.
130
3264-3265
2008
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8
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2
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8
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673689
Namgoong
Co-evolution of the archaeal t ...
Methanothermobacter thermautotrophicus
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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9
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9
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662450
Feng
Gln-tRNAGln formation from Glu ...
Methanothermobacter thermautotrophicus
J. Biol. Chem.
280
8150-8155
2005
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1
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7
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7
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1
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492304
Harpel
Mutagenesis and mechanism-base ...
Streptococcus pyogenes
Biochemistry
41
6398-6407
2002
-
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1
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3
-
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1
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1
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1
1
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1
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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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1
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1
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1
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1
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1
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492302
Horiuchi
Mechanistic studies of reactio ...
Streptococcus pyogenes
Biochemistry
40
6450-6457
2001
1
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5
3
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1
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1
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4
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2
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