BRENDA - Enzyme Database
show all sequences of 2.7.7.59

Cascade control of E. coli glutamine synthetase. II. Metabolite regulation of the enzymes in the cascade

Engleman, E.G.; Francis, S.H.; Arch. Biochem. Biophys. 191, 602-612 (1978)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
glutamine
5 mM, no effect at pH 8.6; pH 7.6, enhances uridylyl removing activity at 0.5 mM
Escherichia coli
Inhibitors
Inhibitors
Commentary
Organism
Structure
3-phosphoglycerate
inhibits uridylyl removing activity
Escherichia coli
acetyl-CoA
inhibits uridylyl removing activity
Escherichia coli
ADP
inhibits uridylyl removing activity
Escherichia coli
AMP
inhibits uridylyl removing activity
Escherichia coli
ATP
inhibits uridylyl removing activity
Escherichia coli
CDP
inhibits uridylyl removing activity
Escherichia coli
CDP-glucose
inhibits uridylyl removing activity
Escherichia coli
CMP
inhibits uridylyl removing activity
Escherichia coli
CoA
inhibits uridylyl removing activity
Escherichia coli
CTP
inhibits uridylyl removing activity
Escherichia coli
D-fructose 1,6-diphosphate
inhibits uridylyl removing activity
Escherichia coli
dCMP
inhibits uridylyl removing activity
Escherichia coli
dUMP
inhibits uridylyl removing activity
Escherichia coli
GDP
inhibits uridylyl removing activity
Escherichia coli
GMP
inhibits uridylyl removing activity
Escherichia coli
GTP
inhibits uridylyl removing activity
Escherichia coli
IDP
inhibits uridylyl removing activity
Escherichia coli
IMP
inhibits uridylyl removing activity
Escherichia coli
ITP
inhibits uridylyl removing activity
Escherichia coli
NAD+
inhibits uridylyl removing activity
Escherichia coli
NADH
inhibits uridylyl removing activity
Escherichia coli
NADP+
inhibits uridylyl removing activity
Escherichia coli
NADPH
inhibits uridylyl removing activity
Escherichia coli
phosphoenolpyruvate
inhibits uridylyl removing activity
Escherichia coli
TDP
inhibits uridylyl removing activity
Escherichia coli
TMP
inhibits uridylyl removing activity
Escherichia coli
TTP
inhibits uridylyl removing activity
Escherichia coli
UDP
inhibits uridylyl removing activity
Escherichia coli
UDP-glucose
inhibits uridylyl removing activity
Escherichia coli
UMP
inhibits uridylyl removing activity
Escherichia coli
UTP
inhibits uridylyl removing activity
Escherichia coli
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mn2+
-
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
UTP + [protein-PII]
Escherichia coli
the enzyme is involved in the cascade control of glutamine synthetase
diphosphate + uridylyl-[protein-PII]
-
Escherichia coli
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
UTP + [protein-PII]
-
643541
Escherichia coli
diphosphate + uridylyl-[protein-PII]
-
643541
Escherichia coli
r
UTP + [protein-PII]
the enzyme is involved in the cascade control of glutamine synthetase
643541
Escherichia coli
diphosphate + uridylyl-[protein-PII]
-
643541
Escherichia coli
r
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
glutamine
5 mM, no effect at pH 8.6; pH 7.6, enhances uridylyl removing activity at 0.5 mM
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
3-phosphoglycerate
inhibits uridylyl removing activity
Escherichia coli
acetyl-CoA
inhibits uridylyl removing activity
Escherichia coli
ADP
inhibits uridylyl removing activity
Escherichia coli
AMP
inhibits uridylyl removing activity
Escherichia coli
ATP
inhibits uridylyl removing activity
Escherichia coli
CDP
inhibits uridylyl removing activity
Escherichia coli
CDP-glucose
inhibits uridylyl removing activity
Escherichia coli
CMP
inhibits uridylyl removing activity
Escherichia coli
CoA
inhibits uridylyl removing activity
Escherichia coli
CTP
inhibits uridylyl removing activity
Escherichia coli
D-fructose 1,6-diphosphate
inhibits uridylyl removing activity
Escherichia coli
dCMP
inhibits uridylyl removing activity
Escherichia coli
dUMP
inhibits uridylyl removing activity
Escherichia coli
GDP
inhibits uridylyl removing activity
Escherichia coli
GMP
inhibits uridylyl removing activity
Escherichia coli
GTP
inhibits uridylyl removing activity
Escherichia coli
IDP
inhibits uridylyl removing activity
Escherichia coli
IMP
inhibits uridylyl removing activity
Escherichia coli
ITP
inhibits uridylyl removing activity
Escherichia coli
NAD+
inhibits uridylyl removing activity
Escherichia coli
NADH
inhibits uridylyl removing activity
Escherichia coli
NADP+
inhibits uridylyl removing activity
Escherichia coli
NADPH
inhibits uridylyl removing activity
Escherichia coli
phosphoenolpyruvate
inhibits uridylyl removing activity
Escherichia coli
TDP
inhibits uridylyl removing activity
Escherichia coli
TMP
inhibits uridylyl removing activity
Escherichia coli
TTP
inhibits uridylyl removing activity
Escherichia coli
UDP
inhibits uridylyl removing activity
Escherichia coli
UDP-glucose
inhibits uridylyl removing activity
Escherichia coli
UMP
inhibits uridylyl removing activity
Escherichia coli
UTP
inhibits uridylyl removing activity
Escherichia coli
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mn2+
-
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
UTP + [protein-PII]
Escherichia coli
the enzyme is involved in the cascade control of glutamine synthetase
diphosphate + uridylyl-[protein-PII]
-
Escherichia coli
r
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
UTP + [protein-PII]
-
643541
Escherichia coli
diphosphate + uridylyl-[protein-PII]
-
643541
Escherichia coli
r
UTP + [protein-PII]
the enzyme is involved in the cascade control of glutamine synthetase
643541
Escherichia coli
diphosphate + uridylyl-[protein-PII]
-
643541
Escherichia coli
r
Other publictions for EC 2.7.7.59
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)
723795
Williams
Adenylylation of mycobacterial ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv, Mycolicibacterium smegmatis, Mycolicibacterium smegmatis ATCC 700084
Tuberculosis
93
198-206
2013
-
-
-
-
-
-
-
-
-
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162
-
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4
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4
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721459
Bonatto
Uridylylation of Herbaspirillu ...
Herbaspirillum seropedicae
Arch. Microbiol.
194
643-652
2012
4
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2
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721679
Jiang
The robustness of the Escheric ...
Escherichia coli
Biochemistry
51
9032-9044
2012
-
-
1
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1
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1
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2
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723230
Yurgel
Nitrogen metabolism in Sinorhi ...
Sinorhizobium meliloti
Mol. Plant Microbe Interact.
25
355-362
2012
-
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6
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1
1
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722521
Zhang
Mutagenesis and functional cha ...
Escherichia coli, Rhodospirillum rubrum
J. Bacteriol.
192
2711-2721
2010
-
-
2
-
11
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2
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5
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2
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11
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2
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702974
Araujo
Different responses of the Gln ...
Azospirillum brasilense
Braz. J. Med. Biol. Res.
41
289-294
2008
2
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1
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2
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674326
Jonsson
In vitro studies of the uridyl ...
Rhodospirillum rubrum, Rhodospirillum rubrum S1
J. Bacteriol.
189
3471-3478
2007
2
-
1
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1
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1
1
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9
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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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1
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2
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1
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1
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676989
Bonatto
Purification and characterizat ...
Herbaspirillum seropedicae
Protein Expr. Purif.
55
293-299
2007
2
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1
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1
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2
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3
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1
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1
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1
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1
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662028
Zhang
GlnD is essential for NifA act ...
Rhodospirillum rubrum
J. Bacteriol.
187
1254-1265
2005
-
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1
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5
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643548
Mutalik
Allosteric interactions and bi ...
Escherichia coli
J. Biol. Chem.
278
26327-26332
2003
-
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643547
Nolden
Sensing nitrogen limitation in ...
Corynebacterium glutamicum
Mol. Microbiol.
42
1281-1295
2001
-
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1
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1
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5
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643549
Colnaghi
Lethality of glnD null mutatio ...
Azotobacter vinelandii
Microbiology
147
1267-1276
2001
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1
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4
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1
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643546
Schlüter
-
The Rhizobium leguminosarum bv ...
Rhizobium leguminosarum
Microbiology
146
2987-2996
2000
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1
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643544
Atkinson
Characterization of the GlnK p ...
Escherichia coli
Mol. Microbiol.
32
301-313
1999
1
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1
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2
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643545
Jakoby
Nitrogen regulation in Coryneb ...
Corynebacterium glutamicum
FEMS Microbiol. Lett.
173
303-310
1999
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643539
Jiang
Reconstitution of the signal-t ...
Escherichia coli
Biochemistry
37
12795-12801
1998
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643538
Johansson
Uridylylation of the PII prote ...
Rhodospirillum rubrum
J. Bacteriol.
179
4190-4194
1997
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643535
Jaggi
The role of the T-loop of the ...
Escherichia coli
FEBS Lett.
391
223-228
1996
-
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643537
Edwards
The role of uridylyltransferas ...
Klebsiella pneumoniae
Mol. Gen. Genet.
247
189-198
1995
-
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1
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1
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3
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1
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643532
Atkinson
Reversible uridylylation of th ...
Escherichia coli
J. Biol. Chem.
269
28288-28293
1994
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643542
van Heeswijk
The genes of the glutamine syn ...
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1993
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643543
Colonna-Romano
Uridylylation of the PII prote ...
Rhizobium leguminosarum
FEBS Lett.
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1993
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643534
Garcia
Cascade control of Escherichia ...
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1983
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643533
Mura
Growth conditions and inactiva ...
Escherichia coli
Boll. Soc. Ital. Biol. Sper.
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1982
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643536
Rhee
New methods for the colorimetr ...
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1978
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643540
Francis
Cascade control of E. coli glu ...
Escherichia coli
Arch. Biochem. Biophys.
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1978
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14
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643541
Engleman
Cascade control of E. coli glu ...
Escherichia coli
Arch. Biochem. Biophys.
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1978
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31
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31
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