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diphosphate + uridylyl-[protein-PII GlnB]
UTP + [protein-PII GlnK]
Substrates: substrate GlnK-UMP3, the enzyme acts on residue Tyr51 of GlnB
Products: -
r
diphosphate + uridylyl-[protein-PII GlnB]
UTP + [protein-PIIGlnB]
diphosphate + uridylyl-[protein-PII GlnK]
UTP + [protein-PII GlnK]
diphosphate + uridylyl-[protein-PII GlnZ]
UTP + [protein-PIIGlnZ]
diphosphate + uridylyl-[protein-PII]
UTP + [protein-PII]
UTP + GlnB
diphosphate + uridylyl-GlnB
UTP + GlnK
diphosphate + uridylyl-GlnK
Substrates: -
Products: -
?
UTP + GlnZ
diphosphate + uridylyl-GlnZ
Substrates: -
Products: -
r
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
UTP + [protein-PII GlnB]
diphosphate + uridylyl-[protein-PII GlnB]
UTP + [protein-PII GlnK]
diphosphate + uridylyl-[protein-PII GlnK]
UTP + [protein-PII GlnZ]
diphosphate + uridylyl-[protein-PII GlnZ]
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
additional information
?
-
diphosphate + uridylyl-[protein-PII GlnB]
UTP + [protein-PIIGlnB]
Substrates: -
Products: -
r
diphosphate + uridylyl-[protein-PII GlnB]
UTP + [protein-PIIGlnB]
Substrates: -
Products: -
r
diphosphate + uridylyl-[protein-PII GlnK]
UTP + [protein-PII GlnK]
Substrates: substrate GlnK-UMP3, the enzyme acts on residue Tyr51 of GlnK
Products: -
r
diphosphate + uridylyl-[protein-PII GlnK]
UTP + [protein-PII GlnK]
Substrates: substrate GlnK-UMP3, the enzyme acts on residue Tyr51 of GlnK
Products: -
r
diphosphate + uridylyl-[protein-PII GlnZ]
UTP + [protein-PIIGlnZ]
Substrates: -
Products: -
r
diphosphate + uridylyl-[protein-PII GlnZ]
UTP + [protein-PIIGlnZ]
Substrates: -
Products: -
r
diphosphate + uridylyl-[protein-PII]
UTP + [protein-PII]
Substrates: -
Products: -
r
diphosphate + uridylyl-[protein-PII]
UTP + [protein-PII]
Substrates: -
Products: -
r
diphosphate + uridylyl-[protein-PII]
UTP + [protein-PII]
Substrates: -
Products: -
r
UTP + GlnB
diphosphate + uridylyl-GlnB
Substrates: -
Products: -
r
UTP + GlnB
diphosphate + uridylyl-GlnB
-
Substrates: -
Products: -
r
UTP + GlnB
diphosphate + uridylyl-GlnB
Substrates: -
Products: -
?
UTP + GlnB
diphosphate + uridylyl-GlnB
Substrates: -
Products: -
r
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
-
Substrates: -
Products: -
r
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
-
Substrates: enzyme is pivotal in sensing intracellular levels of fixed nitrogen
Products: -
r
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
Substrates: GlnK protein mutant Y51F is no substrate
Products: -
?
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
Substrates: uridylylation of GlnK protein is essential for the cell to respond to nitrogen limitation
Products: -
?
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
-
Substrates: regulatory protein
Products: -
ir
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
-
Substrates: GlnK protein mutant Y51N is no substrate
Products: -
ir
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
-
Substrates: very slow reverse reaction
Products: -
ir
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
-
Substrates: GlnK protein wild-type and mutant R47W
Products: -
ir
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
-
Substrates: enzyme regulates the regulatory GlnK protein
Products: -
ir
UTP + [protein-PII GlnB]
diphosphate + uridylyl-[protein-PII GlnB]
Substrates: PII-1 protein
Products: -
r
UTP + [protein-PII GlnB]
diphosphate + uridylyl-[protein-PII GlnB]
Substrates: PII-1 protein
Products: -
r
UTP + [protein-PII GlnB]
diphosphate + uridylyl-[protein-PII GlnB]
Substrates: the enzyme acts on residue Tyr51 of GlnK
Products: -
r
UTP + [protein-PII GlnK]
diphosphate + uridylyl-[protein-PII GlnK]
Substrates: the enzyme acts on residue Tyr51 of GlnK
Products: -
r
UTP + [protein-PII GlnK]
diphosphate + uridylyl-[protein-PII GlnK]
Substrates: the enzyme acts on residue Tyr51 of GlnK
Products: -
r
UTP + [protein-PII GlnZ]
diphosphate + uridylyl-[protein-PII GlnZ]
Substrates: PII-2 protein
Products: -
r
UTP + [protein-PII GlnZ]
diphosphate + uridylyl-[protein-PII GlnZ]
Substrates: PII-2 protein
Products: -
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: -
Products: -
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: enzyme is pivotal in sensing intracellular levels of fixed nitrogen
Products: -
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
Substrates: -
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: -
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
Substrates: unlike in enterobacteria, the enzyme is not the primary nitrogen sensor, overexpression leads to derepression of nitrogen control
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
Substrates: signal transduction cascade model
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
Substrates: the enzyme acts as the primary nitrogen sensor in the nitrogen regulation system
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: -
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: -
Products: -
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
Substrates: -
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
Substrates: -
Products: -
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: mutants Y51F and Y51S are no substrates, Y46F is a poor substrate, structure analysis of the crystallized protein PII variants
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: Tyr51 is the site of uridylation
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: signal transduction cascade model
Products: -
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: the enzyme is involved in the cascade control of glutamine synthetase
Products: -
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: the enzyme is regulated by Gln and controls the activity of PII signal transduction protein
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: the enzyme is regulated by Gln and controls the activity of PII signal transduction protein
Products: -
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: enzyme regulates the adenylyltransferase, which itself regulates the glutamine synthetase by adenylylation and deadenylylation, via protein PII uridylylation and deuridylylation
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: enzyme regulates the adenylyltransferase, which itself regulates the glutamine synthetase by adenylylation and deadenylylation, via protein PII uridylylation and deuridylylation
Products: -
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: nitrogen-regulation of gene transcription results from the regulation of the phosphorylation state of the enhancer-binding transcription factor NRI. Phosphorylation of NRI is regulated by a bicyclic cascade system containing four regulatory proteins, one of which is EC 2.7.7.59
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
Substrates: the enzyme is constitutively expressed at a low level. The functioning of the glutamine synthetase adenylylation cascade is regulated by modulation of the activities of uridylyltransferase and adenylyltransferase, rather than by changes in the expression of their genes
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
Substrates: -
Products: -
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: GlnD of Herbaspirillum seropedicae is overexpressed with the two PII proteins GlnK and GlnB. Results show that GlnD uridylylates GlnB and GlnK trimers producing the forms PII(UMP)1, PII(UMP)2 and PII(UMP)3. GlnB is more efficiently uridylylated than GlnK
Products: -
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
Substrates: -
Products: -
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: -
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: the enzyme is required for derepression of ntr-regulated promoters such as glnAp2 and pnifL, but is not involved in the nif-specific response to changes in nitrogen status mediated by the nifL products
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: the enzyme acts as the primary nitrogen sensor in the nitrogen regulation system
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: -
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
Substrates: -
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: the uridylylation of the PII protein is modulated by the intracellular glutamine/alpha-ketoglutarate ratio
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
Substrates: enzyme is not essential for nitrogen fixation of the host plant
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
Substrates: the enzyme acts as the primary nitrogen sensor in the nitrogen regulation system
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: -
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: GlnD plays an important role in nitrogen assimilation and metabolism by reversibly regulating the modification of PII proteins, which in turn regulate a variety of other proteins. It is essential for NifA activation, NtrB/NtrC-regulated gene expression, and posttranslational regulation of nitrogenase activity
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: bifunctional uridylyltransferase/uridylyl-removing enzyme, in Rhodospirillum rubrum three PII proteins have been identified GlnB, GlnK and GlnJ, respectively, in this study it is shown that all three PII proteins are uridylylated, although the efficacy is dependent on the cation present, Mn2+ or Mg2+, respectively
Products: -
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: bifunctional uridylyltransferase/uridylyl-removing enzyme, in Rhodospirillum rubrum three PII proteins have been identified GlnB, GlnK and GlnJ, respectively, in this study it is shown that all three PII proteins are uridylylated, although the efficacy is dependent on the cation present, Mn2+ or Mg2+, respectively
Products: -
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: -
Products: -
?
additional information
?
-
-
Substrates: regulation
Products: -
?
additional information
?
-
-
Substrates: enzyme is required for the relief of NifL inhibition of NifA under N-limiting conditions
Products: -
?
additional information
?
-
-
Substrates: schematic regulation model
Products: -
?
additional information
?
-
-
Substrates: protein PII is predominantly a ATase regulator protein, while PII and GlnK protein both activate the phosphatase activity of NRII, GlnK protein controls the nitrogen assimilation via ATase in absence of protein PII
Products: -
?
additional information
?
-
Substrates: the bifunctional enzyme GlnD catalyzes the uridylylation and, in the presence of glutamine, the deuridylylation of EcGlnB PII protein
Products: -
-
additional information
?
-
-
Substrates: schematic regulation model
Products: -
?
additional information
?
-
-
Substrates: PII protein GlnK is adenylylated by GlnD in response to nitrogen limitation. In contrast to Escherichia coli, GlnK adenylylation in Mycobyceterium tuberculosis does not regulate glutamine synthetase adenylylation, nor does it mediate the transcriptomic response to nitrogen limitation
Products: -
?
additional information
?
-
-
Substrates: PII protein GlnK is adenylylated by GlnD in response to nitrogen limitation. In contrast to Escherichia coli, GlnK adenylylation in Mycobyceterium tuberculosis does not regulate glutamine synthetase adenylylation, nor does it mediate the transcriptomic response to nitrogen limitation
Products: -
?
additional information
?
-
Substrates: PII protein GlnK is adenylylated by GlnD in response to nitrogen limitation
Products: -
?
additional information
?
-
Substrates: PII protein GlnK is adenylylated by GlnD in response to nitrogen limitation
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
diphosphate + uridylyl-[protein-PII GlnB]
UTP + [protein-PIIGlnB]
diphosphate + uridylyl-[protein-PII GlnZ]
UTP + [protein-PIIGlnZ]
diphosphate + uridylyl-[protein-PII]
UTP + [protein-PII]
UTP + GlnB
diphosphate + uridylyl-GlnB
Substrates: -
Products: -
r
UTP + GlnZ
diphosphate + uridylyl-GlnZ
Substrates: -
Products: -
r
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
UTP + [protein-PII GlnB]
diphosphate + uridylyl-[protein-PII GlnB]
UTP + [protein-PII GlnZ]
diphosphate + uridylyl-[protein-PII GlnZ]
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
additional information
?
-
diphosphate + uridylyl-[protein-PII GlnB]
UTP + [protein-PIIGlnB]
Substrates: -
Products: -
r
diphosphate + uridylyl-[protein-PII GlnB]
UTP + [protein-PIIGlnB]
Substrates: -
Products: -
r
diphosphate + uridylyl-[protein-PII GlnZ]
UTP + [protein-PIIGlnZ]
Substrates: -
Products: -
r
diphosphate + uridylyl-[protein-PII GlnZ]
UTP + [protein-PIIGlnZ]
Substrates: -
Products: -
r
diphosphate + uridylyl-[protein-PII]
UTP + [protein-PII]
Substrates: -
Products: -
r
diphosphate + uridylyl-[protein-PII]
UTP + [protein-PII]
Substrates: -
Products: -
r
diphosphate + uridylyl-[protein-PII]
UTP + [protein-PII]
Substrates: -
Products: -
r
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
-
Substrates: enzyme is pivotal in sensing intracellular levels of fixed nitrogen
Products: -
r
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
Substrates: uridylylation of GlnK protein is essential for the cell to respond to nitrogen limitation
Products: -
?
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
-
Substrates: enzyme regulates the regulatory GlnK protein
Products: -
ir
UTP + [protein-PII GlnB]
diphosphate + uridylyl-[protein-PII GlnB]
Substrates: PII-1 protein
Products: -
r
UTP + [protein-PII GlnB]
diphosphate + uridylyl-[protein-PII GlnB]
Substrates: PII-1 protein
Products: -
r
UTP + [protein-PII GlnZ]
diphosphate + uridylyl-[protein-PII GlnZ]
Substrates: PII-2 protein
Products: -
r
UTP + [protein-PII GlnZ]
diphosphate + uridylyl-[protein-PII GlnZ]
Substrates: PII-2 protein
Products: -
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: enzyme is pivotal in sensing intracellular levels of fixed nitrogen
Products: -
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
Substrates: unlike in enterobacteria, the enzyme is not the primary nitrogen sensor, overexpression leads to derepression of nitrogen control
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
Substrates: signal transduction cascade model
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
Substrates: the enzyme acts as the primary nitrogen sensor in the nitrogen regulation system
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: -
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
Substrates: -
Products: -
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: signal transduction cascade model
Products: -
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: the enzyme is involved in the cascade control of glutamine synthetase
Products: -
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: the enzyme is regulated by Gln and controls the activity of PII signal transduction protein
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: the enzyme is regulated by Gln and controls the activity of PII signal transduction protein
Products: -
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: enzyme regulates the adenylyltransferase, which itself regulates the glutamine synthetase by adenylylation and deadenylylation, via protein PII uridylylation and deuridylylation
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: enzyme regulates the adenylyltransferase, which itself regulates the glutamine synthetase by adenylylation and deadenylylation, via protein PII uridylylation and deuridylylation
Products: -
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: nitrogen-regulation of gene transcription results from the regulation of the phosphorylation state of the enhancer-binding transcription factor NRI. Phosphorylation of NRI is regulated by a bicyclic cascade system containing four regulatory proteins, one of which is EC 2.7.7.59
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
Substrates: the enzyme is constitutively expressed at a low level. The functioning of the glutamine synthetase adenylylation cascade is regulated by modulation of the activities of uridylyltransferase and adenylyltransferase, rather than by changes in the expression of their genes
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
Substrates: -
Products: -
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
Substrates: -
Products: -
r
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: the enzyme is required for derepression of ntr-regulated promoters such as glnAp2 and pnifL, but is not involved in the nif-specific response to changes in nitrogen status mediated by the nifL products
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: the enzyme acts as the primary nitrogen sensor in the nitrogen regulation system
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: the uridylylation of the PII protein is modulated by the intracellular glutamine/alpha-ketoglutarate ratio
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
Substrates: enzyme is not essential for nitrogen fixation of the host plant
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
Substrates: the enzyme acts as the primary nitrogen sensor in the nitrogen regulation system
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: -
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: GlnD plays an important role in nitrogen assimilation and metabolism by reversibly regulating the modification of PII proteins, which in turn regulate a variety of other proteins. It is essential for NifA activation, NtrB/NtrC-regulated gene expression, and posttranslational regulation of nitrogenase activity
Products: -
?
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
-
Substrates: -
Products: -
?
additional information
?
-
-
Substrates: regulation
Products: -
?
additional information
?
-
-
Substrates: enzyme is required for the relief of NifL inhibition of NifA under N-limiting conditions
Products: -
?
additional information
?
-
-
Substrates: schematic regulation model
Products: -
?
additional information
?
-
-
Substrates: protein PII is predominantly a ATase regulator protein, while PII and GlnK protein both activate the phosphatase activity of NRII, GlnK protein controls the nitrogen assimilation via ATase in absence of protein PII
Products: -
?
additional information
?
-
-
Substrates: schematic regulation model
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-oxoglutarate
2-OG, inhibits the UR activity of GlnD
3-phosphoglycerate
-
inhibits uridylyl removing activity
acetyl-CoA
-
inhibits uridylyl removing activity
ADP
-
inhibits uridylyl removing activity
AMP
-
inhibits uridylyl removing activity
ATP
-
inhibits uridylyl removing activity
Cd2+
-
inhibits uridylyl removing activity
CDP
-
inhibits uridylyl removing activity
CDP-glucose
-
inhibits uridylyl removing activity
CMP
-
inhibits uridylyl removing activity
Co2+
-
inhibits uridylyl removing activity
CoA
-
inhibits uridylyl removing activity
CTP
-
inhibits uridylyl removing activity
Cu2+
-
inhibits uridylyl removing activity
D-fructose 1,6-diphosphate
-
inhibits uridylyl removing activity
dCMP
-
inhibits uridylyl removing activity
dUMP
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inhibits uridylyl removing activity
Endogenous inhibitor
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of MW greater than 100000
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GDP
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inhibits uridylyl removing activity
GMP
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inhibits uridylyl removing activity
GTP
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inhibits uridylyl removing activity
IDP
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inhibits uridylyl removing activity
IMP
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inhibits uridylyl removing activity
ITP
-
inhibits uridylyl removing activity
NAD+
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inhibits uridylyl removing activity
NADH
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inhibits uridylyl removing activity
NADP+
-
inhibits uridylyl removing activity
NADPH
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inhibits uridylyl removing activity
Ni2+
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inhibits uridylyl removing activity
phosphoenolpyruvate
-
inhibits uridylyl removing activity
TDP
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inhibits uridylyl removing activity
TMP
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inhibits uridylyl removing activity
TTP
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inhibits uridylyl removing activity
UDP
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inhibits uridylyl removing activity
UDP-glucose
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inhibits uridylyl removing activity
UMP
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inhibits uridylyl removing activity
Zn2+
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inhibits uridylyl removing activity
glutamine
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glutamine
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inhibition of uridylyltransferase activity
glutamine
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shows an inhibition of 65% of GlnB uridylylation and 70% of GlnK uridylylation
glutamine
the presence of glutamine results in increased uridylyl-removing enzyme (UR) activity of GlnD, while it inhibits the uridylyl transferase (UTase) activity of GlnD
UTP
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inhibits uridylyl removing activity
UTP
the higher the UTP concentration, the longer GlnK remains uridylylated with the wild-type enzyme, although not with GlnDDELTAACT mutant
additional information
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no inhibition of uridylyl removing activity by Ba2+, Ca2+, and Mg2+ at 1 mM
-
additional information
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GlnK protein-UMP is a very poor inhibitor of protein PII-UMP deuridylylation
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additional information
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in contrast to Escherichia coli the uridylylation reaction is not inhibited by glutamine
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