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Information on EC 2.7.7.28 - nucleoside-triphosphate-aldose-1-phosphate nucleotidyltransferase
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2.7.7.28 nucleoside-triphosphate-aldose-1-phosphate nucleotidyltransferaseIUBMB Comments
In decreasing order of activity, guanosine, inosine and adenosine diphosphate hexoses are substrates in the reverse reaction, with either glucose or mannose as the sugar.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
hexose nucleotidylating enzyme, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 2.7.7.29
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formerly
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GDP hexose pyrophosphorylase
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GDPhexose pyrophosphorylase
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GTP:alpha-D-hexose-1-phosphate guanylyltransferase
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-
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guanosine diphosphohexose pyrophosphorylase
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guanylyltransferase, hexose 1-phosphate
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hexose 1-phosphate guanylyltransferase
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hexose 1-phosphate nucleotidyltransferase
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hexose nucleotidylating enzyme
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hexose-1-phosphate guanylyltransferase
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NDP hexose pyrophosphorylase
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NTP:hexose-1-phosphate nucleotidyltransferase
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nucleoside diphosphohexose pyrophosphorylase
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nucleoside-triphosphate-hexose-1-phosphate nucleotidyltransferase
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nucleotidyltransferase, hexose 1-phosphate
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nucleoside triphosphate + alpha-D-aldose 1-phosphate = diphosphate + NDP-hexose
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
NTP:alpha-D-aldose-1-phosphate nucleotidyltransferase
In decreasing order of activity, guanosine, inosine and adenosine diphosphate hexoses are substrates in the reverse reaction, with either glucose or mannose as the sugar.
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CAS REGISTRY NUMBER
COMMENTARY
37278-26-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADPmannose + diphosphate
ATP + D-mannose 1-phosphate
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the enzyme catalyzes the pyrophosphorolysis of the following nucleoside diphosphate hexoses in decreasing order of activity: GDPglucose, GDPmannose, IDPmannose, IDPglucose, ADPmannose, UDPglucose and UDPmannose
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-
?
UDPglucose + diphosphate
UTP + D-glucose 1-phosphate
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the enzyme catalyzes the pyrophosphorolysis of the following nucleoside diphosphate hexoses in decreasing order of activity: GDPglucose, GDPmannose, IDPmannose, IDPglucose, ADPmannose, UDPglucose and UDPmannose
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-
?
UDPmannose + diphosphate
UTP + D-mannose 1-phosphate
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the enzyme catalyzes the pyrophosphorolysis of the following nucleoside diphosphate hexoses in decreasing order of activity: GDPglucose, GDPmannose, IDPmannose, IDPglucose, ADPmannose, UDPglucose and UDPmannose
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-
?
GDP-glucose + diphosphate
GTP + D-glucose 1-phosphate
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the enzyme catalyzes the pyrophosphorolysis of the following nucleoside diphosphate hexoses in decreasing order of activity: GDPglucose, GDPmannose, IDPmannose, IDPglucose, ADPmannose, UDPglucose and UDPmannose
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r
GDPmannose + diphosphate
GTP + D-mannose 1-phosphate
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the enzyme catalyzes the pyrophosphorolysis of the following nucleoside diphosphate hexoses in decreasing order of activity: GDPglucose, GDPmannose, IDPmannose, IDPglucose, ADPmannose, UDPglucose and UDPmannose
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-
?
GDPmannose + diphosphate
GTP + D-mannose 1-phosphate
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reaction at about half the rate of GDPglucose
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-
?
IDP-glucose + diphosphate
ITP + D-glucose 1-phosphate
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the enzyme catalyzes the pyrophosphorolysis of the following nucleoside diphosphate hexoses in decreasing order of activity: GDPglucose, GDPmannose, IDPmannose, IDPglucose, ADPmannose, UDPglucose and UDPmannose
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-
?
IDP-glucose + diphosphate
ITP + D-glucose 1-phosphate
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reaction at 21% the rate of GDPglucose
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r
IDPmannose + diphosphate
ITP + D-mannose 1-phosphate
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the enzyme catalyzes the pyrophosphorolysis of the following nucleoside diphosphate hexoses in decreasing order of activity: GDPglucose, GDPmannose, IDPmannose, IDPglucose, ADPmannose, UDPglucose and UDPmannose
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-
r
IDPmannose + diphosphate
ITP + D-mannose 1-phosphate
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reaction at 7% the rate of GDPglucose
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADPmannose + diphosphate
ATP + D-mannose 1-phosphate
-
the enzyme catalyzes the pyrophosphorolysis of the following nucleoside diphosphate hexoses in decreasing order of activity: GDPglucose, GDPmannose, IDPmannose, IDPglucose, ADPmannose, UDPglucose and UDPmannose
-
-
?
UDPglucose + diphosphate
UTP + D-glucose 1-phosphate
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the enzyme catalyzes the pyrophosphorolysis of the following nucleoside diphosphate hexoses in decreasing order of activity: GDPglucose, GDPmannose, IDPmannose, IDPglucose, ADPmannose, UDPglucose and UDPmannose
-
-
?
UDPmannose + diphosphate
UTP + D-mannose 1-phosphate
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the enzyme catalyzes the pyrophosphorolysis of the following nucleoside diphosphate hexoses in decreasing order of activity: GDPglucose, GDPmannose, IDPmannose, IDPglucose, ADPmannose, UDPglucose and UDPmannose
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-
?
GDP-glucose + diphosphate
GTP + D-glucose 1-phosphate
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the enzyme catalyzes the pyrophosphorolysis of the following nucleoside diphosphate hexoses in decreasing order of activity: GDPglucose, GDPmannose, IDPmannose, IDPglucose, ADPmannose, UDPglucose and UDPmannose
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r
GDPmannose + diphosphate
GTP + D-mannose 1-phosphate
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the enzyme catalyzes the pyrophosphorolysis of the following nucleoside diphosphate hexoses in decreasing order of activity: GDPglucose, GDPmannose, IDPmannose, IDPglucose, ADPmannose, UDPglucose and UDPmannose
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?
GDPmannose + diphosphate
GTP + D-mannose 1-phosphate
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reaction at about half the rate of GDPglucose
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?
IDP-glucose + diphosphate
ITP + D-glucose 1-phosphate
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the enzyme catalyzes the pyrophosphorolysis of the following nucleoside diphosphate hexoses in decreasing order of activity: GDPglucose, GDPmannose, IDPmannose, IDPglucose, ADPmannose, UDPglucose and UDPmannose
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-
?
IDP-glucose + diphosphate
ITP + D-glucose 1-phosphate
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reaction at 21% the rate of GDPglucose
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r
IDPmannose + diphosphate
ITP + D-mannose 1-phosphate
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the enzyme catalyzes the pyrophosphorolysis of the following nucleoside diphosphate hexoses in decreasing order of activity: GDPglucose, GDPmannose, IDPmannose, IDPglucose, ADPmannose, UDPglucose and UDPmannose
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-
r
IDPmannose + diphosphate
ITP + D-mannose 1-phosphate
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reaction at 7% the rate of GDPglucose
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?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
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requirement, maximal activity at about 5 mM, maximal activity at about twice the diphosphate-concentration
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
6.5 - 9
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pH 6.5: about 40% of maximal activity, pH 9.0: about half-maximal activity
6.5 - 9
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pH 6.5: about 40% of maximal activity, pH 9.0: about half-maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Verachtert, H.; Rodriguez, P.; Bass, S.T.; Hansen, R.G.
Purification and properties of guanosine diphosphate hexose pyrophosphorylase from mammalian tissues
J. Biol. Chem.
241
2007-2013
1966
Bos taurus, Rattus norvegicus
brenda
Hansen, R.G.; Verachtert, H.; Rodriguez, P.; Bass, S.T.
GDP-hexose pyrophosphorylase from liver
Methods Enzymol.
8
269-271
1966
Bos taurus
-
brenda
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Release 2023.1 (January 2023)
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