BRENDA - Enzyme Database show
show all sequences of 2.7.7.B5

Direct evidence that thil is an ATP pyrophosphatase for the adenylation of uridine in 4-thiouridine biosynthesis

You, D.; Xu, T.; Yao, F.; Zhou, X.; Deng, Z.; ChemBioChem 9, 1879-1882 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Escherichia coli
Engineering
Amino acid exchange
Commentary
Organism
D189A
mutation eliminates in vivo function of the enzyme
Escherichia coli
K321M
mutation eliminates in vivo function of the enzyme
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.24
-
ATP
pH 7.5, 22°C
Escherichia coli
0.84
-
GTP
pH 7.5, 22°C
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Escherichia coli
ThiI is involved in the modification of uridine to 4-thiouridine
?
-
-
-
additional information
Escherichia coli
ThiI plays a role in the transfer of sulfur from cysteine to both thiamine and 4-thiouridine
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Purification (Commentary)
Commentary
Organism
-
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
ThiI is involved in the modification of uridine to 4-thiouridine
691789
Escherichia coli
?
-
-
-
-
additional information
ThiI plays a role in the transfer of sulfur from cysteine to both thiamine and 4-thiouridine
691789
Escherichia coli
?
-
-
-
-
tRNA-uridine + ATP
-
691789
Escherichia coli
adenylated-trNA-uridine + diphosphate
-
-
-
?
tRNA-uridine + ATP
based upon sequence alignments, ThiI shares a unique P-loop motif with the PPi synthetase family. ThiI very likely catalyzes the adenylation of a substrate, probably a molecule bearing a carbonyl oxygen
691789
Escherichia coli
adenylated-trNA-uridine + diphosphate
-
-
-
?
tRNA-uridine + GTP
kcat/Km for GTP is about 6fold lower than the value for ATP
691789
Escherichia coli
adenylated-trNA-uridine + diphosphate
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
22
-
assay at
Escherichia coli
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.113
-
GTP
pH 7.5, 22°C
Escherichia coli
0.604
-
ATP
pH 7.5, 22°C
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Escherichia coli
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D189A
mutation eliminates in vivo function of the enzyme
Escherichia coli
K321M
mutation eliminates in vivo function of the enzyme
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.24
-
ATP
pH 7.5, 22°C
Escherichia coli
0.84
-
GTP
pH 7.5, 22°C
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Escherichia coli
ThiI is involved in the modification of uridine to 4-thiouridine
?
-
-
-
additional information
Escherichia coli
ThiI plays a role in the transfer of sulfur from cysteine to both thiamine and 4-thiouridine
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
-
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
ThiI is involved in the modification of uridine to 4-thiouridine
691789
Escherichia coli
?
-
-
-
-
additional information
ThiI plays a role in the transfer of sulfur from cysteine to both thiamine and 4-thiouridine
691789
Escherichia coli
?
-
-
-
-
tRNA-uridine + ATP
-
691789
Escherichia coli
adenylated-trNA-uridine + diphosphate
-
-
-
?
tRNA-uridine + ATP
based upon sequence alignments, ThiI shares a unique P-loop motif with the PPi synthetase family. ThiI very likely catalyzes the adenylation of a substrate, probably a molecule bearing a carbonyl oxygen
691789
Escherichia coli
adenylated-trNA-uridine + diphosphate
-
-
-
?
tRNA-uridine + GTP
kcat/Km for GTP is about 6fold lower than the value for ATP
691789
Escherichia coli
adenylated-trNA-uridine + diphosphate
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
22
-
assay at
Escherichia coli
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.113
-
GTP
pH 7.5, 22°C
Escherichia coli
0.604
-
ATP
pH 7.5, 22°C
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Escherichia coli
Other publictions for EC 2.7.7.B5
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)
725262
Martinez-Gomez
The rhodanese domain of ThiI i ...
Salmonella enterica
J. Bacteriol.
193
4582-4587
2011
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1
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5
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5
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710548
Tanaka
Deduced RNA binding mechanism ...
Escherichia coli
RNA
15
1498-1506
2009
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1
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1
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1
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1
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691789
You
Direct evidence that thil is a ...
Escherichia coli
ChemBioChem
9
1879-1882
2008
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1
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2
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2
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2
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1
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1
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5
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1
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2
1
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2
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2
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1
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5
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1
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2
1
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694560
Naumann
-
Versuche zur Strukturaufkläru ...
Escherichia coli, Thermotoga maritima
PH. D. Thesis Universität Göttingen
2005
0000
2005
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2
1
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1
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