BRENDA - Enzyme Database
show all sequences of 6.3.5.6

A single amidotransferase forms asparaginyl-tRNA and glutaminyl-tRNA in Chlamydia trachomatis

Raczniak, G.; Becker, H.D.; Min, B.; Söll, D.; J. Biol. Chem. 276, 45862-45867 (2001)

Data extracted from this reference:

Application
Application
Commentary
Organism
pharmacology
enzyme may have potential as a species-specific therapeutic drug target
Chlamydia trachomatis
Cloned(Commentary)
Commentary
Organism
cloning of the gatC, gatA and gatB genes, situated in an operon-like manner, encoding the GatCAB amidotransferase and overexpression in Escherichia coli BL21-Codon Plus-TM
Chlamydia trachomatis
Inhibitors
Inhibitors
Commentary
Organism
Structure
additional information
not inhibited by N-ethylmaleimide, 5,5’-dithiobis(2-nitrobenzoic acid) and p-hydroxymercuribenzoate
Chlamydia trachomatis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
essential for the reaction catalyzed by AdT
Chlamydia trachomatis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
53600
-
1 * 55000, GatA + 1 * 53600, GatB + 1* 11100, GatC, SDS-PAGE
Chlamydia trachomatis
55000
-
1 * 55000, GatA + 1 * 53600, GatB + 1* 11100, GatC, SDS-PAGE
Chlamydia trachomatis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
Asp-tRNAAsn + ?
Chlamydia trachomatis
tRNA-dependent transamidation pathway of Asn-tRNA formation, which is required for protein synthesis or under certain metabolic situations for asparagine synthesis
Asn-tRNAAsn + ?
-
Chlamydia trachomatis
?
Asp-tRNAAsn + ?
Chlamydia trachomatis
it is likely that the dual specificity amidotransferase serves in Asn-tRNA and Gln-tRNA formation in vivo
Asn-tRNAAsn + ?
-
Chlamydia trachomatis
?
Glu-tRNAGln + ?
Chlamydia trachomatis
it is likely that the dual specificity amidotransferase serves in Asn-tRNA and Gln-tRNA formation in vivo
Gln-tRNAGln + ?
-
Chlamydia trachomatis
?
Glu-tRNAGln + ?
Chlamydia trachomatis
tRNA-dependent transamidation pathway of Gln-tRNA formation, which is required for protein synthesis or under certain metabolic situations for glutamine synthesis
Gln-tRNAGln + ?
-
Chlamydia trachomatis
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Chlamydia trachomatis
-
human pathogenic parasite
-
Purification (Commentary)
Commentary
Organism
32fold purification of recombinant enzyme, expressed in Escherichia coli
Chlamydia trachomatis
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.000035
-
-
Chlamydia trachomatis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Asp-tRNAAsn + ?
tRNA-dependent transamidation pathway of Asn-tRNA formation, which is required for protein synthesis or under certain metabolic situations for asparagine synthesis
440092
Chlamydia trachomatis
Asn-tRNAAsn + ?
-
440092
Chlamydia trachomatis
?
Asp-tRNAAsn + ?
it is likely that the dual specificity amidotransferase serves in Asn-tRNA and Gln-tRNA formation in vivo
440092
Chlamydia trachomatis
Asn-tRNAAsn + ?
-
440092
Chlamydia trachomatis
?
ATP + Asp-tRNAAsn + glutamine
dual-specific Asp/Glu-AdT, rates for conversion of Glu to Gln are about twice as fast as the rate of Asp to Asn conversion, enzyme uses glutamine, asparagine or ammonia as amide donors in the presence of ATP, GTP or CTP
440092
Chlamydia trachomatis
ADP + phosphate + Asn-tRNAAsn + glutamate
-
440092
Chlamydia trachomatis
?
ATP + Glu-tRNAGln + glutamine
dual-specific Asp/Glu-AdT, rates for conversion of Glu to Gln are about twice as fast as the rate of Asp to Asn conversion, enzyme uses glutamine, asparagine or ammonia as amide donors in the presence of ATP or GTP
440092
Chlamydia trachomatis
ADP + Gln-tRNAGln + glutamate
-
440092
Chlamydia trachomatis
?
Glu-tRNAGln + ?
it is likely that the dual specificity amidotransferase serves in Asn-tRNA and Gln-tRNA formation in vivo
440092
Chlamydia trachomatis
Gln-tRNAGln + ?
-
440092
Chlamydia trachomatis
?
Glu-tRNAGln + ?
tRNA-dependent transamidation pathway of Gln-tRNA formation, which is required for protein synthesis or under certain metabolic situations for glutamine synthesis
440092
Chlamydia trachomatis
Gln-tRNAGln + ?
-
440092
Chlamydia trachomatis
?
additional information
GatA is likely to be the catalytic subunit, GatB may be responsible for tRNA binding and GatC may be involved in a channeling mechanism, in which the misacylated tRNA formed by the non-discriminating AA-tRNA synthetase could be handed off to the AdT
440092
Chlamydia trachomatis
?
-
-
-
-
additional information
no substrates: correctly charged Asp-tRNAAsp and Glu-tRNAGlu
440092
Chlamydia trachomatis
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
heterotrimer
1 * 55000, GatA + 1 * 53600, GatB + 1* 11100, GatC, SDS-PAGE
Chlamydia trachomatis
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Chlamydia trachomatis
Application (protein specific)
Application
Commentary
Organism
pharmacology
enzyme may have potential as a species-specific therapeutic drug target
Chlamydia trachomatis
Cloned(Commentary) (protein specific)
Commentary
Organism
cloning of the gatC, gatA and gatB genes, situated in an operon-like manner, encoding the GatCAB amidotransferase and overexpression in Escherichia coli BL21-Codon Plus-TM
Chlamydia trachomatis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
additional information
not inhibited by N-ethylmaleimide, 5,5’-dithiobis(2-nitrobenzoic acid) and p-hydroxymercuribenzoate
Chlamydia trachomatis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
essential for the reaction catalyzed by AdT
Chlamydia trachomatis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
53600
-
1 * 55000, GatA + 1 * 53600, GatB + 1* 11100, GatC, SDS-PAGE
Chlamydia trachomatis
55000
-
1 * 55000, GatA + 1 * 53600, GatB + 1* 11100, GatC, SDS-PAGE
Chlamydia trachomatis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
Asp-tRNAAsn + ?
Chlamydia trachomatis
tRNA-dependent transamidation pathway of Asn-tRNA formation, which is required for protein synthesis or under certain metabolic situations for asparagine synthesis
Asn-tRNAAsn + ?
-
Chlamydia trachomatis
?
Asp-tRNAAsn + ?
Chlamydia trachomatis
it is likely that the dual specificity amidotransferase serves in Asn-tRNA and Gln-tRNA formation in vivo
Asn-tRNAAsn + ?
-
Chlamydia trachomatis
?
Glu-tRNAGln + ?
Chlamydia trachomatis
it is likely that the dual specificity amidotransferase serves in Asn-tRNA and Gln-tRNA formation in vivo
Gln-tRNAGln + ?
-
Chlamydia trachomatis
?
Glu-tRNAGln + ?
Chlamydia trachomatis
tRNA-dependent transamidation pathway of Gln-tRNA formation, which is required for protein synthesis or under certain metabolic situations for glutamine synthesis
Gln-tRNAGln + ?
-
Chlamydia trachomatis
?
Purification (Commentary) (protein specific)
Commentary
Organism
32fold purification of recombinant enzyme, expressed in Escherichia coli
Chlamydia trachomatis
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.000035
-
-
Chlamydia trachomatis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Asp-tRNAAsn + ?
tRNA-dependent transamidation pathway of Asn-tRNA formation, which is required for protein synthesis or under certain metabolic situations for asparagine synthesis
440092
Chlamydia trachomatis
Asn-tRNAAsn + ?
-
440092
Chlamydia trachomatis
?
Asp-tRNAAsn + ?
it is likely that the dual specificity amidotransferase serves in Asn-tRNA and Gln-tRNA formation in vivo
440092
Chlamydia trachomatis
Asn-tRNAAsn + ?
-
440092
Chlamydia trachomatis
?
ATP + Asp-tRNAAsn + glutamine
dual-specific Asp/Glu-AdT, rates for conversion of Glu to Gln are about twice as fast as the rate of Asp to Asn conversion, enzyme uses glutamine, asparagine or ammonia as amide donors in the presence of ATP, GTP or CTP
440092
Chlamydia trachomatis
ADP + phosphate + Asn-tRNAAsn + glutamate
-
440092
Chlamydia trachomatis
?
ATP + Glu-tRNAGln + glutamine
dual-specific Asp/Glu-AdT, rates for conversion of Glu to Gln are about twice as fast as the rate of Asp to Asn conversion, enzyme uses glutamine, asparagine or ammonia as amide donors in the presence of ATP or GTP
440092
Chlamydia trachomatis
ADP + Gln-tRNAGln + glutamate
-
440092
Chlamydia trachomatis
?
Glu-tRNAGln + ?
it is likely that the dual specificity amidotransferase serves in Asn-tRNA and Gln-tRNA formation in vivo
440092
Chlamydia trachomatis
Gln-tRNAGln + ?
-
440092
Chlamydia trachomatis
?
Glu-tRNAGln + ?
tRNA-dependent transamidation pathway of Gln-tRNA formation, which is required for protein synthesis or under certain metabolic situations for glutamine synthesis
440092
Chlamydia trachomatis
Gln-tRNAGln + ?
-
440092
Chlamydia trachomatis
?
additional information
GatA is likely to be the catalytic subunit, GatB may be responsible for tRNA binding and GatC may be involved in a channeling mechanism, in which the misacylated tRNA formed by the non-discriminating AA-tRNA synthetase could be handed off to the AdT
440092
Chlamydia trachomatis
?
-
-
-
-
additional information
no substrates: correctly charged Asp-tRNAAsp and Glu-tRNAGlu
440092
Chlamydia trachomatis
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
heterotrimer
1 * 55000, GatA + 1 * 53600, GatB + 1* 11100, GatC, SDS-PAGE
Chlamydia trachomatis
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Chlamydia trachomatis
Other publictions for EC 6.3.5.6
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)
746380
Vijayakumar
Soluble expression and purifi ...
Fasciola gigantica
Protein Expr. Purif.
143
9-13
2018
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1
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728743
Fuengfuloy
Overproduction of the N-termin ...
no activity in Helicobacter pylori
Protein Expr. Purif.
89
25-32
2013
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728397
Fischer
The asparagine-transamidosome ...
Helicobacter pylori
Nucleic Acids Res.
40
4965-4976
2012
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728424
Yu
New WS9326A congeners from Str ...
Brugia malayi
Org. Lett.
14
4946-4949
2012
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4
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1
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715924
Crepin
A hybrid structural model of t ...
Brugia malayi
J. Mol. Biol.
405
1056-1069
2011
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1
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1
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716420
Yu
Tirandamycins from Streptomyce ...
Brugia malayi
Org. Lett.
13
2034-2037
2011
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1
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716885
Polydorides
Computational protein design w ...
Thermus thermophilus
Proteins
79
3448-3468
2011
-
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1
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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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7
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9
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675112
Bernard
Inhibition by L-aspartol adeny ...
Pseudomonas aeruginosa
J. Enzyme Inhib. Med. Chem.
22
77-82
2007
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675931
Bailly
The transamidosome: a dynamic ...
Thermus thermophilus
Mol. Cell
28
228-239
2007
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1
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672190
Chuawong
The nondiscriminating aspartyl ...
Helicobacter pylori
Biochemistry
45
8079-8087
2006
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1
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1
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5
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675227
Ramirez
Brugia malayi asparaginyl-tran ...
Brugia malayi, Homo sapiens
J. Infect. Dis.
193
1164-1171
2006
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2
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2
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677106
Cardoso
A non-discriminating aspartyl- ...
Halobacterium salinarum, Halobacterium salinarum NRC 1
RNA Biol.
3
110-114
2006
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1
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6
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1
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1
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659057
Akochy
Direct glutaminyl-tRNA biosynt ...
Pseudomonas aeruginosa
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767-776
2004
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440091
Tumbula-Hansen
Evolutionary divergence of the ...
Methanothermobacter thermautotrophicus
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37184-37190
2002
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440093
Min
Transfer RNA-dependent amino a ...
Deinococcus radiodurans, Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539, Thermus thermophilus
Proc. Natl. Acad. Sci. USA
99
2678-2683
2002
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440092
Raczniak
A single amidotransferase form ...
Chlamydia trachomatis
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45862-45867
2001
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440090
Becker
The heterotrimeric Thermus the ...
Bacillus subtilis, Deinococcus radiodurans, Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
FEBS Lett.
476
140-144
2000
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440094
Ibba
Aminoacyl-tRNA synthesis ...
Aeropyrum pernix, Archaeoglobus fulgidus, Bacillus subtilis, Deinococcus radiodurans, Methanocaldococcus jannaschii, Methanothermobacter thermautotrophicus, Thermus thermophilus
Annu. Rev. Biochem.
69
617-650
2000
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7
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7
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440095
Tumbula
Domain-specific recruitment of ...
Aeropyrum pernix, Archaeoglobus fulgidus, Bacillus subtilis, Chlamydia trachomatis, Deinococcus radiodurans, Halobacterium salinarum, Helicobacter pylori, Methanocaldococcus jannaschii, Methanosarcina mazei, Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus DELTAH, Saccharolobus solfataricus, Sulfurisphaera tokodaii
Nature
407
106-110
2000
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440087
Curnow
Glutamyl-tRNAGln amidotransfer ...
Bacillus subtilis, Deinococcus radiodurans, Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539, Haloferax volcanii
Proc. Natl. Acad. Sci. USA
95
12838-12843
1998
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