Information on EC 2.7.7.37 - aldose-1-phosphate nucleotidyltransferase

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The expected taxonomic range for this enzyme is: Archaea, Eukaryota

EC NUMBER
COMMENTARY hide
2.7.7.37
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RECOMMENDED NAME
GeneOntology No.
aldose-1-phosphate nucleotidyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NDP + alpha-D-aldose 1-phosphate = phosphate + NDP-aldose
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
UDP-beta-L-arabinose biosynthesis II (from beta-L-arabinose)
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SYSTEMATIC NAME
IUBMB Comments
NDP:alpha-D-aldose-1-phosphate nucleotidyltransferase
The enzyme works on a variety of alpha-D-aldose 1-phosphates and beta-L-aldose 1-phosphates (which have the same anomeric configuration as the former; see 2-Carb-6.2).
CAS REGISTRY NUMBER
COMMENTARY hide
9033-61-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP-mannose + phosphate
ADP + D-mannose 1-phosphate
show the reaction diagram
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30% of activity compared to GDPmannose
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ir
dTDP-glucose + phosphate
dTDP + D-glucose 1-phosphate
show the reaction diagram
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11% of activity compared to GDPmannose
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ir
dTDP-mannose + phosphate
dTDP + D-mannose 1-phosphate
show the reaction diagram
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157% of activity compared to GDPmannose
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ir
GDP-galactose + phosphate
GDP + D-galactose 1-phosphate
show the reaction diagram
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3% of activity compared to GDPmannose
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ir
GDP-mannose + phosphate
GDP + D-mannose 1-phosphate
show the reaction diagram
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-
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ir
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
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-
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?
NDP + aldose 1-phosphate
NDP-aldose + phosphate
show the reaction diagram
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-
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ir
NDP + alpha-D-aldose 1-phosphate
phosphate + NDP-aldose
show the reaction diagram
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-
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?
UDP-acetylglucosamine + phosphate
UDP + N-acetyl-alpha-D-glucosamine 1-phosphate
show the reaction diagram
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5.1% of activity compared to GDPmannose
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ir
UDP-galactose + phosphate
UDP + D-galactose 1-phosphate
show the reaction diagram
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18% of activity compared to GDP-mannose
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ir
UDP-glucose + phosphate
UDP + D-glucose 1-phosphate
show the reaction diagram
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22% of activity compared to GDP-mannose
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ir
UDP-mannose + phosphate
UDP + D-mannose 1-phosphate
show the reaction diagram
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290% of activity compared to GDP-mannose
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ir
UDP-xylose + phosphate
UDP + D-xylose 1-phosphate
show the reaction diagram
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24.5% of activity compared to GDP-mannose
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ir
additional information
?
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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
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
O58649
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?
NDP + aldose 1-phosphate
NDP-aldose + phosphate
show the reaction diagram
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ir
NDP + alpha-D-aldose 1-phosphate
phosphate + NDP-aldose
show the reaction diagram
Q975F9
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?
additional information
?
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O58649
a bifunctional enzyme with phosphomannose isomerase (PMI), EC 5.3.1.8, and mannose-1-phosphate guanylyltransferase (Man-1-P GTase), EC 2.7.7.13, activities, which can synthesize GDP-mannose when accompanied by a phosphomannomutase/phosphoglucomutase (PMM/PGM) enzyme (PH0923). PH0925 protein is a thermostable enzyme with both PMI and multiple sugar-1-P NTase, cf. EC 2.7.7.37, activities. Substrate specificity of the sugar-1-P NTase activity of the PH0925 protein, overview
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
best activating metal ion
Ni2+
activates slightly
Zn2+
highly activating
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-mannose 1-phosphate
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1.25 mM: 22% inhibition, 4.2 mM: 40% inhibition
EDTA
complete inhibition
Mg2+
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17 mM: 32% inhibition
phosphate
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4.5 mM: 55% inhibition
Zn2+
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5 mM: complete inhibition
additional information
the C-terminal 114 residue region of the PH0925 protein inhibits the Man-1-P GTase activity. The phosphomannose isomerase activity is abolished by deletion of the C-terminal 14 residues
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0161
alpha-D-mannose 1-phosphate
pH 7.6, 85°C, recombinant enzyme
6.2
GDP-mannose
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pH 8.0, 30°C
0.0026
GTP
pH 7.6, 85°C, recombinant enzyme
0.12
phosphate
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pH 8.0, 30°C
1.5
UDP-glucose
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pH 8.0, 30°C
0.25
UDP-mannose
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pH 8.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10.2
with GTP and alpha-D-mannose 1-phosphate, purified His-tagged recombinant enzyme, pH 7.6, 85°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9.5
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14% of maximal activity at pH 6.5, 43% of maximal activity at pH 9.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
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assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
additional information
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the enzyme contains the the N-terminal nucleotidylyltransferase domain (residues 1–210) and the C-terminal acetyltransferase domain (residues 211–401), respectively. Comparisons of the crystal structures of the ST0452 protein, PDB ID GGO, and Escherichia coli protein EcGlmU2, PDB ID 2OI5, comparison with ST0452 mutant enzymes, overview. Despite the structural similarities between the N- and C-termini of the ST0452 protein and those of Escherichia coli EcGlmU, the thermostabilities of the two proteins differ greatly, as EcGlmU is a mesophilic enzyme. The structures of these proteins do not correlate directly with their thermostability
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
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15 min: 40% remaining activity, 30 min: 27% remaining activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ultrafiltration or ammonium sulfate precipitation results in heavy loss of activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, concentrated enzyme fraction, stable for several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged PH0925 protein from Escherichia coli strain BL21-Codon Plus(DE3)-RIL by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene PH0925, recombinant expression of His-tagged enzyme PH0925 in Escherichia coli strain BL21-Codon Plus(DE3)-RIL
gene ST0452, recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-Codon Plus(DE3)-RIL
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H308A
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site-directed mutagenesis
K337A
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site-directed mutagenesis
K340A
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site-directed mutagenesis
N331A
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site-directed mutagenesis
Y311A
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site-directed mutagenesis
additional information