Information on EC 2.7.7.59 - [protein-PII] uridylyltransferase

New: Word Map on EC 2.7.7.59
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
2.7.7.59
-
RECOMMENDED NAME
GeneOntology No.
[protein-PII] uridylyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII]
show the reaction diagram
The enzyme uridylates and de-uridylates the small trimeric protein PII
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
UTP:[protein-PII] uridylyltransferase
The enzyme uridylylates and de-uridylylates the small trimeric protein PII. The enzymes from Escherichia coli and Salmonella typhimurium have been wrongly identified, in some databases, as EC 2.7.7.12 (UDP-glucose---hexose-1-phosphate uridylyltransferase), from which it differs greatly in both reaction catalysed and sequence.
CAS REGISTRY NUMBER
COMMENTARY hide
151596-34-8
Escherichia coli clone 21C8 gene glnD reduced
57657-57-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene glnD
-
-
Manually annotated by BRENDA team
gene glnD
-
-
Manually annotated by BRENDA team
putative
UniProt
Manually annotated by BRENDA team
putative
UniProt
Manually annotated by BRENDA team
S1
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UTP + GlnB
diphosphate + uridylyl-GlnB
show the reaction diagram
UTP + GlnK
diphosphate + uridylyl-GlnK
show the reaction diagram
-
-
-
?
UTP + GlnZ
diphosphate + uridylyl-GlnZ
show the reaction diagram
-
-
-
r
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
show the reaction diagram
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UTP + GlnB
diphosphate + uridylyl-GlnB
show the reaction diagram
Q8RQD1
-
-
-
r
UTP + GlnZ
diphosphate + uridylyl-GlnZ
show the reaction diagram
Q8RQD1
-
-
-
r
UTP + [protein-GlnK]
diphosphate + uridylyl-[protein-GlnK]
show the reaction diagram
UTP + [protein-PII]
diphosphate + uridylyl-[protein-PII]
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
-
uridylylation assay with 100 mM KCl
NH4+
uridylylation in response to the concentration of ammonium ions
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
inhibits uridylyl removing activity
Endogenous inhibitor
-
of MW greater than 100000
-
GDP
-
inhibits uridylyl removing activity
glutamine
GMP
-
inhibits uridylyl removing activity
GTP
-
inhibits uridylyl removing activity
IDP
-
inhibits uridylyl removing activity
IMP
-
inhibits uridylyl removing activity
iodoacetamide
-
-
iodoacetate
-
-
ITP
-
inhibits uridylyl removing activity
NAD+
-
inhibits uridylyl removing activity
NADH
-
inhibits uridylyl removing activity
NADP+
-
inhibits uridylyl removing activity
NADPH
-
inhibits uridylyl removing activity
Ni2+
-
inhibits uridylyl removing activity
PCMB
-
inactivation
phosphoenolpyruvate
-
inhibits uridylyl removing activity
TDP
-
inhibits uridylyl removing activity
TMP
-
inhibits uridylyl removing activity
TTP
-
inhibits uridylyl removing activity
UDP
-
inhibits uridylyl removing activity
UDP-glucose
-
inhibits uridylyl removing activity
UMP
-
inhibits uridylyl removing activity
UTP
-
inhibits uridylyl removing activity
Zn2+
-
inhibits uridylyl removing activity
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
ADP
or ATP, absolutely required for in vitro uridylylation of PII proteins GlnB and GlnK. Maximum uridylylation rates for both proteins are observed in the presence of about 2 mM 2-oxoglutarate and 200-500 microM ATP. Uridylylation of both GlnB and GlnK responds to 2-oxoglutarate levels, but only GlnB responds effectively to variation on ADP/ATP ratio
AMP
may partially replace ATP or ADP
glutamine
-
5 mM, no effect at pH 8.6; pH 7.6, enhances uridylyl removing activity at 0.5 mM
L-glutamine
-
stimulates the deuridylylation reaction but in contrast to Escherichia coli glutamine has no effect on the uridylylation reaction
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
steady state model for quantification of sensitivity of glutamine synthetase cascade regulation system system, kinetics
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.6
-
uridylyl-removing activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
94000
-
monomeric enzyme form, HPLC gel filtration
105000
-
deduced from the gene sequence
140000
-
gel filtration
186000
-
dimeric enzyme form, HPLC gel filtration
550000
-
hexameric form, HPLC gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 94000, the enzyme is detected as monomeric, dimeric and hexameric form, HPLC after equilibration with SDS
hexamer
-
6 * 94000, the enzyme is detected as monomeric, dimeric and hexameric form, HPLC after equilibration with SDS
monomer
-
1 * 94000, the enzyme is detected as monomeric, dimeric and hexameric form, HPLC after equilibration with SDS
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing of the purified enzyme results in 35-50% loss of activity
-
purification drastically reduces enzyme stability
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, several months without loss of activity
-
4°C, purified enzyme, in presence of ATP and 0.2 M KCl, 10 h, loss of 15-20% activity compared to storage conditions at -5°C
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1720fold to homogeneity from recombinant overexpressing strain
-
GlnD is expressed as a GST-fusion protein
-
GlnD is less soluble than the purified PII proteins GlnB or GlnK, to improve solubility of GlnD a special buffer is utilised (50 mM Tris-HCl, pH 7.0, 200 mM NaCl, 1 mM DTT) which produces 50% solubilization; protein is purified by anionic exchange chromatography (DEAE-Sepharose column) and gel chromatography (Agarose-Heparin column)
-
on a Hi-trap-chelating-Ni2+ column
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned in Escherichia coli strain RB 9040
-
DNA and amino acid sequence determination and analysis, subcloning in Escherichia coli, recombination of mutant gene into genomic glnD region via double crossover, mutnat VF39-BB3 and VF39-BB1
DNA sequence determination and analysis, overexpression in Escherichia coli strain JM109
-
expression in Echerichia coli RB9065lambdaDE3
-
expression in Escherichia coli
expression of glnD in a deficient mutant strain restores the constitutive enzyme, complementation; gene glnD, construction of chromosomal deletion mutant
gene glnD, DNA and amino acid sequence determination and analysis, chromosome mapping, overexpression and functional complementation in Escherichia coli strain DH5
gene glnD, DNA sequence determination and analysis
gene glnD, overexpression from plasmid in an Escherichia coli strain
-
into the vector pET28a for expression in Escherichia coli cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D107A
-
large decrease in activity
D107V
-
large decrease in activity
D107Y
-
large decrease in activity
G93L
-
large decrease in activity
G93V
-
large decrease in activity
G94L
-
large decrease in activity
G94V
-
large decrease in activity
H514A/D515A
-
large decrease in activity
H514Q/D515N
-
large decrease in activity
additional information
Show AA Sequence (579 entries)
Please use the Sequence Search for a certain query.