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ATP + Asp-tRNAAsn + L-glutamine
ADP + phosphate + Asn-tRNAAsn + L-glutamate
ATP + Glu-tRNAGln + Asn
ADP + phosphate + Gln-tRNAGln + Asp
ATP + Glu-tRNAGln + L-asparagine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
ATP + Glu-tRNAGln + L-glutamine + H2O
ADP + phosphate + Gln-tRNAGln + L-glutamate
ATP + Glu-tRNAGln + NH4Cl
ADP + phosphate + Gln-tRNAGln + ?
ATP + L-aspartyl-tRNAAsn + L-glutamine + H2O
ADP + phosphate + L-asparaginyl-tRNAAsn + L-glutamate
-
-
-
-
?
ATP + L-glutamate + tRNAGln1(UUG)
AMP + diphosphate + L-glutamyl-tRNAGln1(UUG)
-
the enzyme is active toward the two tRNAGln isoacceptors, but with a significant catalytic preference for tRNAGln2(CUG). The less active tRNAGln1(UUG) responds to the less common CAA codon for Gln
-
-
?
ATP + L-glutamate + tRNAGln2(CUG)
AMP + diphosphate + L-glutamyl-tRNAGln2(CUG)
-
the enzyme is active toward the two tRNAGln isoacceptors, but with a significant catalytic preference for tRNAGln2(CUG). The less active tRNAGln1(UUG) responds to the less common CAA codon for Gln. The wild-type enzyme shows a 24fold catalytic preference for tRNAGln2 over tRNAGlu
-
-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
-
?
ATP + L-glutamyl-tRNAGln + L-glutamine
ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
ATP-gammaS + Glu-tRNAGln + L-glutamine
? + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
?
additional information
?
-
ATP + Asp-tRNAAsn + L-glutamine
ADP + phosphate + Asn-tRNAAsn + L-glutamate
-
-
-
?
ATP + Asp-tRNAAsn + L-glutamine
ADP + phosphate + Asn-tRNAAsn + L-glutamate
-
-
-
-
?
ATP + Asp-tRNAAsn + L-glutamine
ADP + phosphate + Asn-tRNAAsn + L-glutamate
-
the enzyme transamidates Asp-tRNAAsn and Glu-tRNAGln with similar efficiency
-
-
?
ATP + Asp-tRNAAsn + L-glutamine
ADP + phosphate + Asn-tRNAAsn + L-glutamate
-
identity elements used by GatCAB to discriminate tRNAAsn from tRNAAsp. GatCAB specifically binds Asp-tRNAAsn. Therefore, modified nucleotides do not play an essential role in GatCAB discrimination of Asp-tRNAAsn from Asp-tRNAAsp
-
-
?
ATP + Glu-tRNAGln + Asn
ADP + phosphate + Gln-tRNAGln + Asp
-
Asn is much less effective as amide donor than glutamine
-
-
?
ATP + Glu-tRNAGln + Asn
ADP + phosphate + Gln-tRNAGln + Asp
-
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
the amidation of Glu-tRNAGln proceeds via a gamma-phosphorylated intermediate
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
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
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
the enzyme transamidates Asp-tRNAAsn and Glu-tRNAGln with similar efficiency. GatCAB uses the amide donor glutamine 129fold more efficiently than asparagine
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
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
-
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
Ser176A is the active-site nucleophile for facilitating Gln hydrolysis by the enzyme
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
organisms lacking Gln-tRNA synthetase produce Gln-tRNAGln from misacylated Glu-tRNAGln through the transamidation activity of Glu-tRNAGln amidotransferase. The enzyme hydrolyzes Gln to Glu and NH3, using the latter product to transamidate Glu-tRNAGln in concert with ATP hydrolysis
-
?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
the enzyme produces Gln-tRNAGln required for plastidal protein biosynthesis
-
-
?
ATP + Glu-tRNAGln + L-glutamine + H2O
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
-
?
ATP + Glu-tRNAGln + L-glutamine + H2O
ADP + phosphate + Gln-tRNAGln + L-glutamate
-
-
-
-
?
ATP + Glu-tRNAGln + NH4Cl
ADP + phosphate + Gln-tRNAGln + ?
-
NH4Cl is much less effective as amide donor than glutamine
-
-
?
ATP + Glu-tRNAGln + NH4Cl
ADP + phosphate + Gln-tRNAGln + ?
-
-
-
-
?
ATP + L-glutamyl-tRNAGln + L-glutamine
ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
A0A509AHQ9; A0A509AM58
-
-
-
?
ATP + L-glutamyl-tRNAGln + L-glutamine
ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
A0A509AHQ9; A0A509AM58
-
-
-
?
ATP + L-glutamyl-tRNAGln + L-glutamine
ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
-
-
-
?
ATP + L-glutamyl-tRNAGln + L-glutamine
ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
-
-
-
?
ATP + L-glutamyl-tRNAGln + L-glutamine
ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
-
-
-
-
?
additional information
?
-
-
the enzyme possesses low glutaminase activity
-
-
?
additional information
?
-
-
the association of archaeal glutamyl-tRNA synthetase (ND-GluRS) with GatDE sequesters the tRNA synthetase for Gln-tRNAGln formation, with GatDE reducing the affinity of glutamyl-tRNA synthetase (ND-GluRS) for tRNAGlu 13fold
-
-
?
additional information
?
-
A0A509AHQ9; A0A509AM58
no substrate: L-glutamate
-
-
?
additional information
?
-
A0A509AHQ9; A0A509AM58
no substrate: L-glutamate
-
-
?
additional information
?
-
no substrate: L-glutamate
-
-
?
additional information
?
-
-
in absence of the amido acceptor, Glu-tRNAGln, the enzyme has basal glutaminase activity that is unaffected by ATP
-
-
?
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(1R,2R)-1-(4-methylsulfonylphenyl)-2-(S-dioxo-L-methioneamido)-1,3-propanediol
-
-
(1R,2R)-1-(4-nitrophenyl)-2-(S-dioxo-L-methioneamido)-1,3-propanediol
-
-
(1R,2R)-1-phenyl-2-(S-dioxo-L-methioneamido)-1,3-propanediol
-
-
(1R,2S)-1-(4-nitrophenyl)-2-(S-dioxo-L-methioneamido)-1,3-propanediol
-
-
(1S,2R)-1-(4-nitrophenyl)-2-(S-dioxo-L-methioneamido)-1,3-propanediol
-
-
(1S,2S)-1-(4-nitrophenyl)-2-(S-dioxo-L-methioneamido)-1,3-propanediol
-
-
2'-O-(trinitrophenyl)adenosine 5'-triphosphate
-
IC50: 2.4 mM
3'-(L-alpha-aspartylamino)-3'-deoxy-N,N-dimethyladenosine
-
puromycin analogue
3'-deoxy-3'-(L-alpha-glutamylamino)-N,N-dimethyladenosine
-
puromycin analogue
3'-deoxy-3'-(L-glutaminylamino)-N,N-dimethyladenosine
-
puromycin analogue
3'-O-(trinitrophenyl)adenosine 5'-triphosphate
-
IC50: 2.4 mM
3'-[[(2S)-2-amino-4-(methylsulfinyl)butanoyl]amino]-3'-deoxy-N,N-dimethyladenosine
-
puromycin analogue
3'-[[(2S)-2-amino-4-(methylsulfonyl)butanoyl]amino]-3'-deoxy-N,N-dimethyladenosine
-
puromycin analogue
3'-[[(2S)-4-carboxy-2-hydroxybutanoyl]amino]-3'-deoxy-N,N-dimethyladenosine
-
puromycin analogue
3'-[[2-amino-4-(methylphosphinato)butanoyl]amino]-3'-deoxy-N,N-dimethyladenosine
-
puromycin analogue
6-diazo-5-oxonorleucine
-
blocking of glutamine-dependent reaction, no inhibition of ammonia-dependent reaction
adenosine 5'-[beta,gamma-methylene]triphosphate
-
IC50: 2.3 mM
ATP-gammaS
-
IC50: 0.19 mM
gamma-Glu boronic acid
-
IC50: 0.0016 mM
L-methionine-S-sulfoximine
-
at 1 mM, 3 mM or 5 mM, 20% inhibition
puromycin
-
aminonucleoside antibiotic produced by Streptomyces alboniger, very weak inhibitor of AdT
additional information
-
no inhibition by 6-diazo-5-oxonorleucine
-
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0.12
(1R,2R)-1-(4-methylsulfonylphenyl)-2-(S-dioxo-L-methioneamido)-1,3-propanediol
-
pH 7, temperature not specified in the publication
0.027
(1R,2R)-1-(4-nitrophenyl)-2-(S-dioxo-L-methioneamido)-1,3-propanediol
-
pH 7, temperature not specified in the publication
0.4
(1R,2R)-1-phenyl-2-(S-dioxo-L-methioneamido)-1,3-propanediol
-
pH 7, temperature not specified in the publication
0.37
(1R,2S)-1-(4-nitrophenyl)-2-(S-dioxo-L-methioneamido)-1,3-propanediol
-
pH 7, temperature not specified in the publication
2.8
(1S,2R)-1-(4-nitrophenyl)-2-(S-dioxo-L-methioneamido)-1,3-propanediol
-
pH 7, temperature not specified in the publication
0.16
(1S,2S)-1-(4-nitrophenyl)-2-(S-dioxo-L-methioneamido)-1,3-propanediol
-
pH 7, temperature not specified in the publication
0.134
3'-(L-alpha-aspartylamino)-3'-deoxy-N,N-dimethyladenosine
-
-
0.105
3'-deoxy-3'-(L-alpha-glutamylamino)-N,N-dimethyladenosine
-
-
0.045
3'-deoxy-3'-(L-glutaminylamino)-N,N-dimethyladenosine
-
-
0.011
3'-[[(2S)-2-amino-4-(methylsulfinyl)butanoyl]amino]-3'-deoxy-N,N-dimethyladenosine
-
-
0.004
3'-[[(2S)-2-amino-4-(methylsulfonyl)butanoyl]amino]-3'-deoxy-N,N-dimethyladenosine
-
-
0.13
3'-[[(2S)-4-carboxy-2-hydroxybutanoyl]amino]-3'-deoxy-N,N-dimethyladenosine
-
-
0.033
3'-[[2-amino-4-(methylphosphinato)butanoyl]amino]-3'-deoxy-N,N-dimethyladenosine
-
-
1.85
chloramphenicol
-
pH 7, temperature not specified in the publication
4.1
puromycin
-
very weak inhibitor of AdT
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K236E/E328A
-
mutant used for crystallization, secondary structure contents and enzymatic activities similar to wild-type
S128T
-
mutant protein retains significant glutaminase activity and transamidase activity in the presence of Gln
S152A
-
mutant is glutaminase inactive
S152T
-
mutant is glutaminase inactive
D178E
-
glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable
D178N
-
glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable
K254E
-
glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable
T101A
-
glutamine hydrolysis is negligible, Gln-tRNAGln formation is undetectable
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
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
T177V
-
glutamine hydrolysis is negligible. Gln-tRNAGln formation is undetectable
E125D
mutation in subunit B, molecular dynamics simulations
E125Q
mutation in subunit B, molecular dynamics simulations
K88R
mutation in subunit B, molecular dynamics simulations
T175V
mutation in subunit B, molecular dynamics simulations
E125D
-
mutation in subunit B, molecular dynamics simulations
-
E125Q
-
mutation in subunit B, molecular dynamics simulations
-
K88R
-
mutation in subunit B, molecular dynamics simulations
-
T175V
-
mutation in subunit B, molecular dynamics simulations
-
additional information
-
activity of the engineered enzyme variants indicates that the acceptor stem loop is the principle discrimination element because insertion of this loop alone enhances the specificity of the archaeal enzyme toward tRNAGln2
additional information
construction of an an N-terminal deletion mutant lacking amino acids 1-186 corresponding to the eukaryote-specific protein domains. The domains substantially influence amino acid binding, tRNA binding and aminoacylation efficiency, but they play no role in either specific nucleotide readout or discrimination against noncognate tRNA
additional information
-
construction of an an N-terminal deletion mutant lacking amino acids 1-186 corresponding to the eukaryote-specific protein domains. The domains substantially influence amino acid binding, tRNA binding and aminoacylation efficiency, but they play no role in either specific nucleotide readout or discrimination against noncognate tRNA
-
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Vothknecht, U.C.; Doernemann, D.
Charging of both, plastidial tRNAgln and tRNAglu with glutamate and subsequent amidation of the misacylated tRNAgln by a glutamyl-tRNA amidotransferase in the unicellular green alga Scenedesmus obliquus, mutant C-2A'
Z. Naturforsch. C
50
789-795
1995
Tetradesmus obliquus
-
brenda
Horiuchi, K.Y.; Harpel, M.R.; Shen, L.; Luo, Y.; Rogers, K.C.; Copeland, R.A.
Mechanistic studies of reaction coupling in Glu-tRNAGln amidotransferase
Biochemistry
40
6450-6457
2001
Streptococcus pyogenes
brenda
Curnow, A.W.; Hong, K.W.; Yuan, R.; Kim, S.I.; Martins, O.; Winkler, W.; Henkin, T.M.; Soll, D.
Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation
Proc. Natl. Acad. Sci. USA
94
11819-11826
1997
Bacillus subtilis
brenda
Harpel, M.R.; Horiuchi, K.Y.; Luo, Y.; Shen, L.; Jiang, W.; Nelson, D.J.; Rogers, K.C.; Decicco, C.P.; Copeland, R.A.
Mutagenesis and mechanism-based inhibition of Streptococcus pyogenes Glu-tRNAGln amidotransferase implicate a serine-based glutaminase site
Biochemistry
41
6398-6407
2002
Streptococcus pyogenes
brenda
Kwak, J.H.; Shin, K.; Woo, J.S.; Kim, M.K.; Kim, S.I.; Eom, S.H.; Hong, K.W.
Expression, purification, and crystallization of glutamyl-tRNA(Gln) specific amidotransferase from Bacillus stearothermophilus
Mol. Cells
14
374-381
2002
Geobacillus stearothermophilus
brenda
Jahn, D.; Kim, Y.C.; Ishino, Y.; Chen, M.W.; Soll, D.
Purification and functional characterization of the Glu-tRNAGln amidotransferase from Chlamydomonas reinhardtii
J. Biol. Chem.
265
8059-8064
1990
Chlamydomonas reinhardtii
brenda
Zalkin, H.
Glu-tRNAGln amidotransferase
Methods Enzymol.
113
303-305
1985
Bacillus subtilis
brenda
Salazar, J.C.; Zuniga, R.; Raczniak, G.; Becker, H.; Soll, D.; Orellana, O.
A dual-specific Glu-tRNA(Gln) and Asp-tRNA(Asn) amidotransferase is involved in decoding glutamine and asparagine codons in Acidithiobacillus ferrooxidans
FEBS Lett.
500
129-131
2001
Acidithiobacillus ferrooxidans
brenda
Strauch, M.A.; Zalkin, H.; Aronson, A.I.
Characterization of the glutamyl-tRNAGln-to-glutaminyl-tRNAGln amidotransferase reaction of Bacillus subtilis
J. Bacteriol.
170
916-920
1988
Bacillus subtilis
brenda
Feng, L.; Sheppard, K.; Tumbula-Hansen, D.; Soell, D.
Gln-tRNAGln formation from Glu-tRNAGln requires cooperation of an asparaginase and a Glu-tRNAGln kinase
J. Biol. Chem.
280
8150-8155
2005
Methanothermobacter thermautotrophicus
brenda
Namgoong, S.; Sheppard, K.; Sherrer, R.L.; Soell, D.
Co-evolution of the archaeal tRNA-dependent amidotransferase GatCAB with tRNAAsn
FEBS Lett.
581
309-314
2007
Methanothermobacter thermautotrophicus
brenda
Sheppard, K.; Akochy, P.M.; Salazar, J.C.; Soell, D.
The Helicobacter pylori amidotransferase GatCAB is equally efficient in glutamine-dependent transamidation of Asp-tRNAAsn and Glu-tRNAGln
J. Biol. Chem.
282
11866-11873
2007
Helicobacter pylori
brenda
Balg, C.; Huot, J.L.; Lapointe, J.; Chenevert, R.
Inhibition of Helicobacter pylori Aminoacyl-tRNA Amidotransferase by Puromycin Analogues
J. Am. Chem. Soc.
130
3264-3265
2008
Helicobacter pylori
brenda
Nagao, A.; Suzuki, T.; Katoh, T.; Sakaguchi, Y.; Suzuki, T.
Biogenesis of glutaminyl-mt tRNAGln in human mitochondria
Proc. Natl. Acad. Sci. USA
106
16209-16214
2009
Homo sapiens (O43716), Homo sapiens (O75879), Homo sapiens (Q9H0R6)
brenda
Chatani, M.; Tanaka, M.; Nakamura, A.; Takesue, N.; Tanaka, I.; Asano, K.
A simple turbidimetric method for monitoring the inhibition of tRNA-dependent amidotransferase GatCAB
J. Microbiol. Methods
80
117-122
2010
Staphylococcus aureus
brenda
Balg, C.; De Mieri, M.; Huot, J.L.; Blais, S.P.; Lapointe, J.; Chenevert, R.
Inhibition of Helicobacter pylori aminoacyl-tRNA amidotransferase by chloramphenicol analogs
Bioorg. Med. Chem.
18
7868-7872
2010
Helicobacter pylori
brenda
Ito, T.; Yokoyama, S.
Two enzymes bound to one transfer RNA assume alternative conformations for consecutive reactions
Nature
467
612-616
2010
Thermotoga maritima (Q9X0Z9)
brenda
Rampias, T.; Sheppard, K.; Soell, D.
The archaeal transamidosome for RNA-dependent glutamine biosynthesis
Nucleic Acids Res.
38
5774-5783
2010
Methanothermobacter thermautotrophicus
brenda
Grant, T.D.; Luft, J.R.; Wolfley, J.R.; Snell, M.E.; Tsuruta, H.; Corretore, S.; Quartley, E.; Phizicky, E.M.; Grayhack, E.J.; Snell, E.H.
The structure of yeast glutaminyl-tRNA synthetase and modeling of its interaction with tRNA
J. Mol. Biol.
425
2480-2493
2013
Thermotoga maritima
brenda
Huot, J.L.; Fischer, F.; Corbeil, J.; Madore, E.; Lorber, B.; Diss, G.; Hendrickson, T.L.; Kern, D.; Lapointe, J.
Gln-tRNAGln synthesis in a dynamic transamidosome from Helicobacter pylori, where GluRS2 hydrolyzes excess Glu-tRNAGln
Nucleic Acids Res.
39
9306-9315
2011
Helicobacter pylori
brenda
O'Donoghue, P.; Sheppard, K.; Nureki, O.; Soell, D.
Rational design of an evolutionary precursor of glutaminyl-tRNA synthetase
Proc. Natl. Acad. Sci. USA
108
20485-20490
2011
Methanothermobacter thermautotrophicus
brenda
Chongdar, N.; Dasgupta, S.; Datta, A.B.; Basu, G.
Preliminary X-ray crystallographic analysis of an engineered glutamyl-tRNA synthetase from Escherichia coli
Acta Crystallogr. Sect. F
70
922-927
2014
Escherichia coli
brenda
Echevarria, L.; Clemente, P.; Hernandez-Sierra, R.; Gallardo, M.E.; Fernandez-Moreno, M.A.; Garesse, R.
Glutamyl-tRNAGln amidotransferase is essential for mammalian mitochondrial translation invivo
Biochem. J.
460
91-101
2014
Mus musculus (Q9CZN8), Mus musculus
brenda
Mailu, B.M.; Li, L.; Arthur, J.; Nelson, T.M.; Ramasamy, G.; Fritz-Wolf, K.; Becker, K.; Gardner, M.J.
Plasmodium apicoplast Gln-tRNAGln biosynthesis utilizes a unique GatAB amidotransferase essential for erythrocytic stage parasites
J. Biol. Chem.
290
29629-29641
2015
Plasmodium berghei (A0A509AHQ9 and A0A509AM58), Plasmodium berghei ANKA (A0A509AHQ9 and A0A509AM58), Plasmodium falciparum (Q8I1S6 and C6KTC3)
brenda
Hadd, A.; Perona, J.J.
Coevolution of specificity determinants in eukaryotic glutamyl- and glutaminyl-tRNA synthetases
J. Mol. Biol.
426
3619-3633
2014
Saccharomyces cerevisiae (P13188)
brenda
Dewage, S.W.; Cisneros, G.A.
Computational analysis of ammonia transfer along two intramolecular tunnels in Staphylococcus aureus glutamine-dependent amidotransferase (GatCAB)
J. Phys. Chem. B
119
3669-3677
2015
Staphylococcus aureus (P63488 and P64201), Staphylococcus aureus ATCC 700699 (P63488 and P64201)
brenda