BRENDA - Enzyme Database show
show all sequences of 6.3.5.7

A simple turbidimetric method for monitoring the inhibition of tRNA-dependent amidotransferase GatCAB

Chatani, M.; Tanaka, M.; Nakamura, A.; Takesue, N.; Tanaka, I.; Asano, K.; J. Microbiol. Methods 80, 117-122 (2010)

Data extracted from this reference:

Application
Application
Commentary
Organism
analysis
simple system for monitoring the inhibition of GatCAB activity using Escherichia coli Top10 co-expressing the non-discriminating glutamyl-tRNA synthetase ndGluRS and GatCAB genes from Staphylococcus aureus Mu50. Growth repression is confirmed by introducing ndgluRS from Staphylococcus aureus Mu50 into Escherichia coli. Co-expression of the gatCAB operon alleviates growth repression in the host Escherichia coli. The screening system consists of these two transformants and non-expressing Escherichia coli Top10. The transformant harbors both ndGluRS gene and GatCAB operon can be co-expressed in the presence and in the absence of chemical compounds of interest. There is no inhibitor that inactivates GatCAB activity, but upon expression of two inactive GatCAB deletion variants, GatCAB-10 and GatCAB-CHD, together with ndGluRS in Escherichia coli Top10, the cells show repressed growth as well as ndGluRS is expressed
Staphylococcus aureus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Staphylococcus aureus
-
-
-
Application (protein specific)
Application
Commentary
Organism
analysis
simple system for monitoring the inhibition of GatCAB activity using Escherichia coli Top10 co-expressing the non-discriminating glutamyl-tRNA synthetase ndGluRS and GatCAB genes from Staphylococcus aureus Mu50. Growth repression is confirmed by introducing ndgluRS from Staphylococcus aureus Mu50 into Escherichia coli. Co-expression of the gatCAB operon alleviates growth repression in the host Escherichia coli. The screening system consists of these two transformants and non-expressing Escherichia coli Top10. The transformant harbors both ndGluRS gene and GatCAB operon can be co-expressed in the presence and in the absence of chemical compounds of interest. There is no inhibitor that inactivates GatCAB activity, but upon expression of two inactive GatCAB deletion variants, GatCAB-10 and GatCAB-CHD, together with ndGluRS in Escherichia coli Top10, the cells show repressed growth as well as ndGluRS is expressed
Staphylococcus aureus
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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Mailu
Plasmodium apicoplast Gln-tRN ...
Plasmodium berghei, Plasmodium berghei ANKA, Plasmodium falciparum
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Preliminary X-ray crystallogr ...
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922-927
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Echevarria
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Mus musculus
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2014
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Hadd
Coevolution of specificity de ...
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The structure of yeast glutami ...
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Gln-tRNAGln synthesis in a dyn ...
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A simple turbidimetric method ...
Staphylococcus aureus
J. Microbiol. Methods
80
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2010
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Thermotoga maritima
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2010
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The archaeal transamidosome fo ...
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Gln-tRNAGln formation from Glu ...
Methanothermobacter thermautotrophicus
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492304
Harpel
Mutagenesis and mechanism-base ...
Streptococcus pyogenes
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6398-6407
2002
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Expression, purification, and ...
Geobacillus stearothermophilus
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2002
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Horiuchi
Mechanistic studies of reactio ...
Streptococcus pyogenes
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2001
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Salazar
A dual-specific Glu-tRNA(Gln) ...
Acidithiobacillus ferrooxidans
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500
129-131
2001
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492303
Curnow
Glu-tRNAGln amidotransferase: ...
Bacillus subtilis
Proc. Natl. Acad. Sci. USA
94
11819-11826
1997
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Vothknecht
-
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789-795
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492306
Jahn
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492310
Strauch
Characterization of the glutam ...
Bacillus subtilis
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170
916-920
1988
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492307
Zalkin
Glu-tRNAGln amidotransferase ...
Bacillus subtilis
Methods Enzymol.
113
303-305
1985
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