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2-deoxy-D-glucose 6-phosphate
2-deoxy-D-glucose 1-phosphate
-
-
-
-
?
2-deoxyribose 1-phosphate
2-deoxyribose 5-phosphate
-
-
-
-
?
3-phospho-D-glyceric acid
?
-
no mutase activity
-
-
?
alpha-D-glucose 1,6-bisphosphate
?
-
-
-
-
?
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
alpha-D-mannose-1-phosphate
D-mannose-6-phosphate
-
-
-
-
r
D-fructose-1-phosphate
D-fructose-6-phosphate
-
no mutase activity
-
-
?
D-glucosamine-1-phosphate
D-glucosamine-6-phosphate
-
low enzyme activity
-
-
?
D-glucose 1-phosphate
D-glucose 6-phosphate
D-glucose-1-phosphate
D-glucose-6-phosphate
D-Mannose 1-phosphate
D-Mannose 6-phosphate
D-mannose 6-phosphate
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
D-mannose 1-phosphate
D-mannose-1-phosphate
D-mannose-6-phosphate
D-mannose-1-phosphate
mannose-6-phosphate
-
-
-
-
r
Glucose 1-phosphate
Glucose 6-phosphate
N-acetyl-D-glucosamine-1-phosphate
N-acetyl-D-glucosamine-6-phosphate
-
no mutase activity
-
-
?
additional information
?
-
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
?
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
-
?
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
?
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
-
?
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
-
-
?
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
-
-
-
-
?
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
-
-
-
?
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
-
-
-
-
?
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
-
-
-
?
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
-
-
-
?
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
-
-
-
r
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
-
-
-
-
?
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
-
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
20fold higher activity than with alpha-D-glucose 1-phosphate
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
the interconversion occurs via a mannose-1,6-(bis) phosphate intermediate
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
PMM/PGM catalyzes the second step in alginate biosynthesis
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
second step of the alginate biosynthetic pathway
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
20fold higher activity than with alpha-D-glucose 1-phosphate
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
preferred substrate
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
preferred substrate
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
the enzyme also catalyzes the interconversion of alpha-D-glucose 1-phosphate to D-glucose 6-phosphate
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
best substrate
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
best substrate
-
-
?
D-glucose 1-phosphate
D-glucose 6-phosphate
reaction with mannose 1-phosphate is more efficient than with D-glucose-1-phosphate
-
-
?
D-glucose 1-phosphate
D-glucose 6-phosphate
-
-
-
?
D-glucose 1-phosphate
D-glucose 6-phosphate
-
-
-
-
?
D-glucose-1-phosphate
D-glucose-6-phosphate
-
-
-
?
D-glucose-1-phosphate
D-glucose-6-phosphate
-
-
-
-
r
D-glucose-1-phosphate
D-glucose-6-phosphate
-
-
-
-
r
D-glucose-1-phosphate
D-glucose-6-phosphate
-
-
-
-
r
D-glucose-1-phosphate
D-glucose-6-phosphate
-
bifunctional enzyme
-
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
-
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
reaction with mannose 1-phosphate is more efficient than with D-glucose-1-phosphate
-
-
r
D-Mannose 1-phosphate
D-Mannose 6-phosphate
Cassia corymbosa
-
r
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
the cosubstrate glucose-1,6-diphosphate or mannose 1,6-diphosphate is converted to the corresponding sugar monophosphate while the substrate is converted to the sugar biphosphate in each reaction cycle
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
the cosubstrate glucose-1,6-diphosphate or mannose 1,6-diphosphate is converted to the corresponding sugar monophosphate while the substrate is converted to the sugar biphosphate in each reaction cycle
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
-
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
-
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
-
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
-
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
enzyme is activated by transfer of a phosphate group from glucose 1,6-diphosphate or mannose 1,6-diphosphate
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
-
-
-
r
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
r
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
-
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
-
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
-
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
r
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
more slowly in the reverse direction
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
-
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
-
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
-
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
-
-
?
D-mannose 6-phosphate
alpha-D-mannose 1-phosphate
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
D-mannose 6-phosphate
alpha-D-mannose 1-phosphate
the enzyme also catalyzes the interconversion of alpha-D-glucose 1-phosphate to D-glucose 6-phosphate
-
-
?
D-mannose 6-phosphate
D-mannose 1-phosphate
-
-
-
r
D-mannose 6-phosphate
D-mannose 1-phosphate
-
conversion to mannose 1-phosphate, which is a substrate for the synthesis of GDPmannose. This nucleotide sugar is then used in the synthesis of dolichol-phosphate-mannose, which is essential for N-linked glycosylation and thus the secretion of several glycoproteins as well as for the synthesis of glycosyl-phosphatidyl-inositol anchored proteins
-
-
?
D-mannose 6-phosphate
D-mannose 1-phosphate
-
first enzyme of the N-glycosylation pathway
-
-
?
D-mannose 6-phosphate
D-mannose 1-phosphate
-
-
-
-
r
D-mannose 6-phosphate
D-mannose 1-phosphate
-
the enzyme produces mannose 1-phosphate for the synthesis of mannose-1,6-diphosphate as well as of GDPmannose
-
-
?
D-mannose 6-phosphate
D-mannose 1-phosphate
-
the enzyme is required for synthesis of lipopolysaccharide O side chains
-
-
?
D-mannose-1-phosphate
D-mannose-6-phosphate
-
-
-
-
r
D-mannose-1-phosphate
D-mannose-6-phosphate
-
-
-
-
r
D-mannose-1-phosphate
D-mannose-6-phosphate
-
bifunctional enzyme
-
-
?
Glucose 1-phosphate
Glucose 6-phosphate
-
-
-
?
Glucose 1-phosphate
Glucose 6-phosphate
-
-
-
?
additional information
?
-
D-glucose 1,6-bisphosphate and D-mannose 1,6-bisphosphate can be hydrolyzed by isoform PMM1
-
-
?
additional information
?
-
D-glucose 1,6-bisphosphate and D-mannose 1,6-bisphosphate can be hydrolyzed by isoform PMM1
-
-
?
additional information
?
-
-
D-glucose 1,6-bisphosphate and D-mannose 1,6-bisphosphate can be hydrolyzed by isoform PMM1
-
-
?
additional information
?
-
-
PMM1 is less specific: it has nearly equal phosphomannomutase and phosphoglucomutase activities as well as a modest glucose-1,6-bisphosphatase activity corresponding to about 3% of its phosphomannomutase activity
-
-
?
additional information
?
-
-
bifunctional enzyme with phosphoglucomutase, EC 5.4.2.2, and phosphomannomutase activities
-
-
?
additional information
?
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities, the catalytic efficiency is about 15fold higher for glucose 1-phosphate than for mannose 1-phosphate
-
-
?
additional information
?
-
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities, the catalytic efficiency is about 15fold higher for glucose 1-phosphate than for mannose 1-phosphate
-
-
?
additional information
?
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities, the catalytic efficiency is about 15fold higher for glucose 1-phosphate than for mannose 1-phosphate
-
-
?
additional information
?
-
the enzyme exhibits the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphomannomutase, EC 5.4.2.8, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview
-
-
?
additional information
?
-
-
the enzyme exhibits the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphomannomutase, EC 5.4.2.8, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview
-
-
?
additional information
?
-
the enzyme exhibits the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphomannomutase, EC 5.4.2.8, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
-
r
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
D-mannose 6-phosphate
alpha-D-mannose 1-phosphate
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
D-mannose 6-phosphate
D-mannose 1-phosphate
additional information
?
-
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
PMM/PGM catalyzes the second step in alginate biosynthesis
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
second step of the alginate biosynthetic pathway
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
20fold higher activity than with alpha-D-glucose 1-phosphate
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
?
D-mannose 6-phosphate
D-mannose 1-phosphate
-
conversion to mannose 1-phosphate, which is a substrate for the synthesis of GDPmannose. This nucleotide sugar is then used in the synthesis of dolichol-phosphate-mannose, which is essential for N-linked glycosylation and thus the secretion of several glycoproteins as well as for the synthesis of glycosyl-phosphatidyl-inositol anchored proteins
-
-
?
D-mannose 6-phosphate
D-mannose 1-phosphate
-
first enzyme of the N-glycosylation pathway
-
-
?
D-mannose 6-phosphate
D-mannose 1-phosphate
-
the enzyme produces mannose 1-phosphate for the synthesis of mannose-1,6-diphosphate as well as of GDPmannose
-
-
?
D-mannose 6-phosphate
D-mannose 1-phosphate
-
the enzyme is required for synthesis of lipopolysaccharide O side chains
-
-
?
additional information
?
-
-
bifunctional enzyme with phosphoglucomutase, EC 5.4.2.2, and phosphomannomutase activities
-
-
?
additional information
?
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities, the catalytic efficiency is about 15fold higher for glucose 1-phosphate than for mannose 1-phosphate
-
-
?
additional information
?
-
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities, the catalytic efficiency is about 15fold higher for glucose 1-phosphate than for mannose 1-phosphate
-
-
?
additional information
?
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities, the catalytic efficiency is about 15fold higher for glucose 1-phosphate than for mannose 1-phosphate
-
-
?
additional information
?
-
the enzyme exhibits the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphomannomutase, EC 5.4.2.8, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview
-
-
?
additional information
?
-
-
the enzyme exhibits the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphomannomutase, EC 5.4.2.8, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview
-
-
?
additional information
?
-
the enzyme exhibits the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphomannomutase, EC 5.4.2.8, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview
-
-
?
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
alpha-D-Glucose 1,6-bisphosphate
-
alpha-D-glucose 1,6-diphosphate
alpha-D-mannose 1,6-bisphosphate
-
alpha-D-Mannose 1,6-diphosphate
D-Glucose 1,6-bisphosphate
D-Mannose 1,6-bisphosphate
histidine
Cassia corymbosa
-
required, maximal activation at 10 mM
inosine monophosphate
the phosphatase activity of isoform PMM1 is enhanced by inosine monophosphate
Insulin
-
incubation with insulin for 45min led to a more than twofold activation of the enzyme
-
alpha-D-glucose 1,6-diphosphate
-
required
alpha-D-glucose 1,6-diphosphate
Cassia corymbosa
-
Km: 0.00087 mM
alpha-D-glucose 1,6-diphosphate
Cassia corymbosa
-
or alpha-D-mannose 1,6-diphosphate required
alpha-D-glucose 1,6-diphosphate
-
the cosubstrate glucose 1,6-diphosphate is converted to the corresponding sugar monophosphate while the substrate is converted to the sugar biphosphate in each reaction cycle
alpha-D-glucose 1,6-diphosphate
-
or alpha-D-mannose 1,6-diphosphate required
alpha-D-glucose 1,6-diphosphate
-
enzyme is activated by transfer of a phosphate group from glucose 1,6-diphosphate
alpha-D-glucose 1,6-diphosphate
-
or alpha-D-mannose 1,6-diphosphate required
alpha-D-glucose 1,6-diphosphate
-
Km: 0.0003 mM
alpha-D-glucose 1,6-diphosphate
-
required
alpha-D-glucose 1,6-diphosphate
-
Km: 0.15 mM
alpha-D-glucose 1,6-diphosphate
-
or alpha-D-mannose 1,6-diphosphate required
alpha-D-glucose 1,6-diphosphate
-
Km: 0.16 mM
alpha-D-glucose 1,6-diphosphate
-
or alpha-D-mannose 1,6-diphosphate required
alpha-D-Mannose 1,6-diphosphate
Cassia corymbosa
-
or alpha-D-glucose 1,6-diphosphate required
alpha-D-Mannose 1,6-diphosphate
Cassia corymbosa
-
Km: 0.0025 mM
alpha-D-Mannose 1,6-diphosphate
-
the cosubstrate glucose 1,6-diphosphate is converted to the corresponding sugar monophosphate while the substrate is converted to the sugar biphosphate in each reaction cycle
alpha-D-Mannose 1,6-diphosphate
-
or alpha-D-glucose 1,6-diphosphate required
alpha-D-Mannose 1,6-diphosphate
-
enzyme is activated by transfer of a phosphate group from mannose 1,6-diphosphate
alpha-D-Mannose 1,6-diphosphate
-
Km: 0.0003 mM
alpha-D-Mannose 1,6-diphosphate
-
or alpha-D-glucose 1,6-diphosphate required
alpha-D-Mannose 1,6-diphosphate
-
or alpha-D-glucose 1,6-diphosphate required
alpha-D-Mannose 1,6-diphosphate
-
or alpha-D-glucose 1,6-diphosphate required
alpha-D-Mannose 1,6-diphosphate
-
Km: 0.12 mM
D-Glucose 1,6-bisphosphate
in presence of 0.02 and 0.2 mM mannose 1-phosphate substrate, half-maximal stimulation of recombinant enzyme at 0.004 and 0.008 mM D-glucose 1,6-bisphosphate
D-Glucose 1,6-bisphosphate
-
D-Glucose 1,6-bisphosphate
-
D-Glucose 1,6-bisphosphate
-
PMM2 requires a hexose bisphosphate for activity, as potent as mannose 1,6-bisphosphate in activation
D-Glucose 1,6-bisphosphate
required for activity
D-Glucose 1,6-bisphosphate
-
-
D-Mannose 1,6-bisphosphate
-
D-Mannose 1,6-bisphosphate
-
PMM2 requires a hexose bisphosphate for activity, as potent as glucose 1,6-bisphosphate in activation, half-maximal activation in the presence of 0.01 mM and 0.1 mM at 0.0005 mM and 0.001 mM mannose 1,6-bisphosphate, respectively
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3.5
2-deoxyribose-1-phosphate
-
90°C
0.006 - 0.4516
alpha-D-glucose 1-phosphate
0.0056 - 1.37
alpha-D-mannose 1-phosphate
0.0075 - 0.0654
D-glucose 1-phosphate
0.0135 - 3
D-glucose-1-phosphate
0.018 - 0.15
D-mannose 1-phosphate
0.3 - 0.5
D-mannose 6-phosphate
Cassia corymbosa
-
-
0.016 - 3.2
D-mannose-1-phosphate
0.0013 - 0.022
glucose 1-phosphate
0.003 - 0.2
mannose 1-phosphate
0.074
mannose 6-phosphate
-
in presence of glucose 1,6-diphosphate
additional information
additional information
-
KM mannose-1-phosphate isoenzyme PH0923S101A not detectable, 37°C
-
0.006
alpha-D-glucose 1-phosphate
-
recombinant enzyme PMM1
0.0073
alpha-D-glucose 1-phosphate
isoform PMM1, at pH 7.5 and 32°C
0.0082
alpha-D-glucose 1-phosphate
isoform PMM2, at pH 7.5 and 32°C
0.012
alpha-D-glucose 1-phosphate
-
-
0.0127
alpha-D-glucose 1-phosphate
-
mutant RN110A
0.0132
alpha-D-glucose 1-phosphate
-
mutant R15A
0.0195
alpha-D-glucose 1-phosphate
-
mutant R247A
0.0272
alpha-D-glucose 1-phosphate
wild type enzyme, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0273
alpha-D-glucose 1-phosphate
-
wild-type
0.0279
alpha-D-glucose 1-phosphate
-
mutant R421C
0.028
alpha-D-glucose 1-phosphate
-
at pH 7.5 and 35°C
0.0354
alpha-D-glucose 1-phosphate
mutant enzyme P368A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0366
alpha-D-glucose 1-phosphate
mutant enzyme S369A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0489
alpha-D-glucose 1-phosphate
mutant enzyme P368G, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0491
alpha-D-glucose 1-phosphate
mutant enzyme R262A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0493
alpha-D-glucose 1-phosphate
mutant enzyme Y17A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0518
alpha-D-glucose 1-phosphate
mutant enzyme E325A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0667
alpha-D-glucose 1-phosphate
mutant enzyme R262A/P368G, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.4516
alpha-D-glucose 1-phosphate
-
in 50 mM Tris-HCl (pH 7.5), at 37°C
0.0056
alpha-D-mannose 1-phosphate
-
in 50 mM HEPES, pH 7.1, 5 mM MgCl2, at 30°C
0.0065
alpha-D-mannose 1-phosphate
isoform PMM1, at pH 7.5 and 32°C
0.017
alpha-D-mannose 1-phosphate
-
at pH 7.5 and 35°C
0.0237
alpha-D-mannose 1-phosphate
isoform PMM2, at pH 7.5 and 32°C
0.068
alpha-D-mannose 1-phosphate
-
mutant enzyme G7R/R37Q, at 28°C
0.111
alpha-D-mannose 1-phosphate
-
mutant enzyme R37Q, at 28°C
0.1569
alpha-D-mannose 1-phosphate
-
in 50 mM Tris-HCl (pH 7.5), at 37°C
0.2
alpha-D-mannose 1-phosphate
-
wild type enzyme, at 28°C
0.204
alpha-D-mannose 1-phosphate
-
mutant enzyme G7R/R37Q, at 18°C
0.229
alpha-D-mannose 1-phosphate
-
mutant enzyme G7R, at 28°C
0.294
alpha-D-mannose 1-phosphate
-
mutant enzyme R37Q, at 18°C
0.327
alpha-D-mannose 1-phosphate
pH 7.3, 37°C
0.387
alpha-D-mannose 1-phosphate
-
wild type enzyme, at 18°C
0.4
alpha-D-mannose 1-phosphate
isoform PMM-D1, 30°C, pH not specified in the publication
0.46
alpha-D-mannose 1-phosphate
isoform PMM-A1, 37°C, pH not specified in the publication
0.475
alpha-D-mannose 1-phosphate
-
mutant enzyme G7R, at 18°C
0.48
alpha-D-mannose 1-phosphate
isoform PMM-D2, 30°C, pH not specified in the publication
0.68
alpha-D-mannose 1-phosphate
recombinant His-tagged enzyme, pH 7.6, temperature not specified in the publication
1.37
alpha-D-mannose 1-phosphate
-
-
0.0075
D-glucose 1-phosphate
isoform alpha-PMM1, pH 6.5, 25°C
0.0654
D-glucose 1-phosphate
30°C, pH 7.5
0.0135
D-glucose-1-phosphate
isoform alpha-PMM2, pH 6.5, 25°C
0.0952
D-glucose-1-phosphate
-
isoenzyme PH0923, 65°C
0.127
D-glucose-1-phosphate
-
isoenzyme PH0923S101A, 65°C
3
D-glucose-1-phosphate
-
90°C
0.018
D-mannose 1-phosphate
-
-
0.0297
D-mannose 1-phosphate
30°C, pH 7.5
0.054
D-mannose 1-phosphate
isoform alpha-PMM1, pH 6.5, 25°C
0.15
D-mannose 1-phosphate
Cassia corymbosa
-
-
0.016
D-mannose-1-phosphate
isoform alpha-PMM2, pH 6.5, 25°C
0.0915
D-mannose-1-phosphate
-
isoenzyme PH0923, 37°C
3.2
D-mannose-1-phosphate
-
90°C
0.0013
glucose 1-phosphate
H308N/H329N double mutant
0.0013
glucose 1-phosphate
S108A mutant
0.0024
glucose 1-phosphate
S108A/H308N double mutant
0.0027
glucose 1-phosphate
K118L/H109Q double mutant
0.0028
glucose 1-phosphate
R20A mutant
0.0034
glucose 1-phosphate
S108D mutant
0.008
glucose 1-phosphate
H109Q mutant
0.008
glucose 1-phosphate
K118L mutant
0.009
glucose 1-phosphate
R247A mutant
0.01
glucose 1-phosphate
H308N mutant
0.01
glucose 1-phosphate
S108V mutant
0.012
glucose 1-phosphate
-
0.016
glucose 1-phosphate
H329N mutant
0.022
glucose 1-phosphate
-
-
0.003
mannose 1-phosphate
-
-
0.0032
mannose 1-phosphate
-
recombinant enzyme PMM1
0.016
mannose 1-phosphate
-
in presence of glucose 1,6-diphosphate
0.06
mannose 1-phosphate
-
-
0.2
mannose 1-phosphate
-
-
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G7R
-
mutant exhibits activity similar to wild type enzyme
G7R/R37Q
-
temperature-sensitive Arabidopsis thaliana PMM-12 mutant (G7R/R37Q) has lower PMM protein and enzyme activity levels than the wild type enzyme
R37Q
-
mutant exhibits decreased activity similar to wild type enzyme
C241S
the mutant shows 60% residual activity the mutation is associated with phosphomannomutase 2 deficiency
D188G |
mutant of isoform PMM2, 2% of wild-type activiy, involved in congential disorder of glycosylation type 1a
D209G
inactive, the mutation is associated with phosphomannomutase 2 deficiency
E197A
the mutant has wild type activity
F157S
inactive, the mutation is associated with phosphomannomutase 2 deficiency
F207S
inactive, the mutation is associated with phosphomannomutase 2 deficiency
L32R
the mutant shows 45% residual activity the mutation is associated with phosphomannomutase 2 deficiency
P113L
the mutant shows 43% residual activity, the mutation is associated with phosphomannomutase 2 deficiency
P184T
inactive, the mutation is associated with phosphomannomutase 2 deficiency
R123Q
inactive, the mutation is associated with phosphomannomutase 2 deficiency
R141H/F119L
the stability-impaired mutant has wild type activity
R162W
mutant of isoform PMM2, involved in congential disorder of glycosylation type 1a
T118S
the mutant shows 1% residual activity the mutation is associated with phosphomannomutase 2 deficiency
T237M
the mutant shows 48% residual activity the mutation is associated with phosphomannomutase 2 deficiency
V129M
mutant of isoform PMM2, involved in congential disorder of glycosylation type 1a
V231M
mutant of isoform PMM2, loss of stability at 40°C, involved in congential disorder of glycosylation type 1a
V44A
the mutant shows 16% residual activity the mutation is associated with phosphomannomutase 2 deficiency
E325A
mutant shows 0.08% of wild type activity
H109Q
6% of wild-type activity
H308N
100% of wild-type activity
H308N/H329N
5% of wild-type activity
H329N
6% of wild-type activity
K118L
4% of wild-type activity
K118L/H109Q
5% of wild-type activity
N110A
-
no remarkable differences in Km and Vmax value compared to wild-type, but intermediate glucose-1,6-bisphosphate dissociates from mutant 25times more often than from wild-type
P368A
mutant shows 10% of wild type activity
P368G
mutant shows 8.7% of wild type activity
R15A
-
no remarkable differences in Km and Vmax value compared to wild-type, but intermediate glucose-1,6-bisphosphate dissociates from mutant 25times more often than from wild-type
R241C
-
0.3% of wild-type acivity, with Km value similar to wild-type
R262A
mutant shows 6.1% of wild type activity
R262A/P368G
mutant shows 2.5% of wild type activity
S108
crystal structure, 5% of wild-type activity
S108A
12% of wild-type activity
S108A/H109Q
6% of wild-type activity
S108A/H308N
3% of wild-type activity
S108D
7% of wild-type activity
S108V
1% of wild-type activity
S10V
5% of wild-type activity
S369A
mutant shows 20.5% of wild type activity
Y17A
mutant shows 0.35% of wild type activity
DELTAmanAB
phosphomannose isomerase, phosphomannosemutase double mutant
D65Y
mutant of isoform PMM2, involved in congential disorder of glycosylation type 1a
D65Y
the mutant shows 20% residual activity the mutation is associated with phosphomannomutase 2 deficiency
F119L
mutant of isoform PMM2, involved in congential disorder of glycosylation type 1a
F119L
the mutant shows reduced activity compared to the wild type enzyme
R141H
inactive
R141H
mutant of isoform PMM2, 0.4% of wild-type activiy, involved in congential disorder of glycosylation type 1a
R141H
inactive, the mutation is associated with phosphomannomutase 2 deficiency
R141H
the mutation lowers activity to approximately one hundredth of that of wild type enzyme
R20A
-
no catalytic activity
R20A
12% of wild-type activity
R247A
9% of wild-type activity
R247A
-
no remarkable differences in Km and Vmax value compared to wild-type, modest increase in dissociation of intermediate glucose-1,6-bisphosphate from enzyme
S101A
-
mutant protein PH0923S101A to investigate the role of the serine residue
S101A
-
mutant protein PH0923S101A to investigate the role of the serine residue
-
additional information
expression as green fluorescent protein fusion protein in Arabidospsis thaliana increases ascorbic acid content by 25-33%
additional information
-
expression in Leishmania mexicana does not restore virulence of an enzyme deletion mutant
additional information
enzyme knock-out mutant is avirulent
additional information
-
enzyme knock-out mutant is avirulent
additional information
-
reducing enzyme expression level through virus-induced gene silencing causes substantial decrease in ascorbic acid content in leaves. Raising the expression level leads to 20-50% increase in ascorbic acid content
additional information
RNAi knockdown of gene TbPMM, construction of a cell line expressing tetracycline inducible double-stranded RNA targeting TbPMM, induction of dsRNA targeting TbPMM results in a 68% knockdown of TbPMM mRNA after 48 h and a reduction of growth rate that leads to cell death after 72 h, phenotypes, overview
additional information
-
RNAi knockdown of gene TbPMM, construction of a cell line expressing tetracycline inducible double-stranded RNA targeting TbPMM, induction of dsRNA targeting TbPMM results in a 68% knockdown of TbPMM mRNA after 48 h and a reduction of growth rate that leads to cell death after 72 h, phenotypes, overview
additional information
-
RNAi knockdown of gene TbPMM, construction of a cell line expressing tetracycline inducible double-stranded RNA targeting TbPMM, induction of dsRNA targeting TbPMM results in a 68% knockdown of TbPMM mRNA after 48 h and a reduction of growth rate that leads to cell death after 72 h, phenotypes, overview
-
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Inhibition of phosphomannose isomerase by fructose 1-phosphate: an explanation for defective N-glycosylation in hereditary fructose intolerance
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The synthesis of mannose 1-phosphate in brain
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Phosphomannomutase activity in wild-type and alginate-producing strains of Pseudomonas aeruginosa
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The yeast SEC53 gene encodes phosphomannomutase
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Kinetic mechanism and pH dependence of the kinetic parameters of Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase
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288
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Among multiple phosphomannomutase gene orthologues, only one gene encodes a protein with phosphoglucomutase and phosphomannomutase activities in Thermococcus kodakaraensis
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Characterization of a thermostable enzyme with phosphomannomutase/phosphoglucomutase activities from the hyperthermophilic archaeon Pyrococcus horikoshii OT3
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138
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Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor
Acta Crystallogr. Sect. F
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Pseudomonas aeruginosa
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Ray, W.K.; Keith, S.M.; DeSantis, A.M.; Hunt, J.P.; Larson, T.J.; Helm, R.F.; Kennelly, P.J.
A phosphohexomutase from the archaeon Sulfolobus solfataricus is covalently modified by phosphorylation on serine
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The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal the structural basis of congenital disorder of glycosylation type 1a
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281
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Pseudomonas aeruginosa
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Kedzierski, L.; Malby, R.L.; Smith, B.J.; Perugini, M.A.; Hodder, A.N.; Ilg, T.; Colman, P.M.; Handman, E.
Structure of Leishmania mexicana phosphomannomutase highlights similarities with human isoforms
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2006
Homo sapiens, Leishmania mexicana (Q95ZD7), Leishmania mexicana
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Qian, W.; Yu, C.; Qin, H.; Liu, X.; Zhang, A.; Johansen, I.E.; Wang, D.
Molecular and functional analysis of phosphomannomutase (PMM) from higher plants and genetic evidence for the involvement of PMM in ascorbic acid biosynthesis in Arabidopsis and Nicotiana benthamiana
Plant J.
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Nicotiana benthamiana, Arabidopsis thaliana (O80840)
brenda
Schramm, A.M.; Mehra-Chaudhary, R.; Furdui, C.M.; Beamer, L.J.
Backbone flexibility, conformational change, and catalysis in a phosphohexomutase from Pseudomonas aeruginosa
Biochemistry
47
9154-9162
2008
Pseudomonas aeruginosa (P26276)
brenda
Yoon, S.; Park, S.; Kim, Y.; Shin, M.; Chong, C.; Choi, J.
Cloning and characterization of phosphoglucomutase and phosphomannomutase derived from Sphingomonas chungbukensis DJ77
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2008
Sphingobium chungbukense, Sphingobium chungbukense DJ77
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Veiga-da-Cunha, M.; Vleugels, W.; Maliekal, P.; Matthijs, G.; Van Schaftingen, E.
Mammalian phosphomannomutase PMM1 is the brain IMP-sensitive glucose-1,6-bisphosphatase
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2008
Mus musculus
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Hoeberichts, F.A.; Vaeck, E.; Kiddle, G.; Coppens, E.; van de Cotte, B.; Adamantidis, A.; Ormenese, S.; Foyer, C.H.; Zabeau, M.; Inze, D.; Perilleux, C.; Van Breusegem, F.; Vuylsteke, M.
A temperature-sensitive mutation in the Arabidopsis thaliana phosphomannomutase gene disrupts protein glycosylation and triggers cell death
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Arabidopsis thaliana
brenda
Nic Lochlainn, L.; Caffrey, P.
Phosphomannose isomerase and phosphomannomutase gene disruptions in Streptomyces nodosus: impact on amphotericin biosynthesis and implications for glycosylation engineering
Metab. Eng.
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Streptomyces nodosus (B6Z254), Streptomyces nodosus
brenda
Badejo, A.A.; Eltelib, H.A.; Fukunaga, K.; Fujikawa, Y.; Esaka, M.
Increase in ascorbate content of transgenic tobacco plants overexpressing acerola (Malpighia glabra) phosphomannomutase gene
Plant Cell Physiol.
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Malpighia glabra (C0JP35), Malpighia glabra
brenda
Siddique, S.; Endres, S.; Atkins, J.M.; Szakasits, D.; Wieczorek, K.; Hofmann, J.; Blaukopf, C.; Urwin, P.E.; Tenhaken, R.; Grundler, F.M.; Kreil, D.P.; Bohlmann, H.
Myo-inositol oxygenase genes are involved in the development of syncytia induced by Heterodera schachtii in Arabidopsis roots
New Phytol.
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Arabidopsis thaliana (O80840)
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Yang, Y.H.; Song, E.; Park, S.H.; Kim, J.N.; Lee, K.; Kim, E.; Kim, Y.G.; Kim, B.G.
Loss of phosphomannomutase activity enhances actinorhodin production in Streptomyces coelicolor
Appl. Microbiol. Biotechnol.
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2010
Streptomyces coelicolor (Q9KZL6), Streptomyces coelicolor
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Yang, Y.; Kang, Y.; Kim, D.; Lee, T.; Park, S.; Lee, K.; Yoo, D.; Liou, K.; Lee, H.; Sohng, J.; Kim, B.
One-pot enzymatic synthesis of deoxy-thymidine-diphosphate (TDP)-2-deoxy-alpha-D-glucose using phosphomannomutase
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Escherichia coli K-12
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brenda
Higashidani, A.; Bode, L.; Nishikawa, A.; Freeze, H.H.
Exogenous mannose does not raise steady state mannose-6-phosphate pools of normal or N-glycosylation-deficient human fibroblasts
Mol. Genet. Metab.
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2009
Homo sapiens, Mus musculus
brenda
Yu, C.; Li, Y.; Li, B.; Liu, X.; Hao, L.; Chen, J.; Qian, W.; Li, S.; Wang, G.; Bai, S.; Ye, H.; Qin, H.; Shen, Q.; Chen, L.; Zhang, A.; Wang, D.
Molecular analysis of phosphomannomutase (PMM) genes reveals a unique PMM duplication event in diverse Triticeae species and the main PMM isozymes in bread wheat tissues
BMC Plant Biol.
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214
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Hordeum vulgare, Oryza sativa, Triticum turgidum subsp. durum, Triticum turgidum subsp. durum (C8CK11), Triticum turgidum subsp. durum (C8CK12), Triticum turgidum subsp. durum (C8CK13), Triticum urartu, Brachypodium distachyon, Triticum aestivum (C8CK06), Triticum aestivum (C8CK09), Triticum aestivum (C8CK10), Triticum aestivum, Aegilops tauschii (C8CK15), Aegilops tauschii (C8CK16)
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Mitra, S.; Cui, J.; Robbins, P.W.; Samuelson, J.
A deeply divergent phosphoglucomutase (PGM) of Giardia lamblia has both PGM and phosphomannomutase activities
Glycobiology
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1233-1240
2010
Giardia intestinalis
brenda
Vega, A.I.; Perez-Cerda, C.; Abia, D.; Gamez, A.; Briones, P.; Artuch, R.; Desviat, L.R.; Ugarte, M.; Perez, B.
Expression analysis revealing destabilizing mutations in phosphomannomutase 2 deficiency (PMM2-CDG): Expression analysis of PMM2-CDG mutations
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Homo sapiens (O15305), Homo sapiens
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Chu, H.Y.; Zheng, Q.C.; Li, X.; Zhao, Y.S.; Zhang, J.L.; Zhang, H.X.
DFT investigation on the reaction mechanism catalyzed by alpha-phosphomannomutase1 in protonated/deprotonated states
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Homo sapiens (Q92871)
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Huang, H.; Li, X.; Wu, M.; Wang, S.; Li, G.; Ma, T.
Cloning, expression and characterization of a phosphoglucomutase/phosphomannomutase from sphingan-producing Sphingomonas sanxanigenens
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Sphingomonas sanxanigenens (M1T754), Sphingomonas sanxanigenens, Sphingomonas sanxanigenens NX02 (M1T754)
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Lee, Y.; Villar, M.T.; Artigues, A.; Beamer, L.J.
Promotion of enzyme flexibility by dephosphorylation and coupling to the catalytic mechanism of a phosphohexomutase
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Pseudomonas aeruginosa
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Bandini, G.; Marino, K.; Guether, M.L.; Wernimont, A.K.; Kuettel, S.; Qiu, W.; Afzal, S.; Kelner, A.; Hui, R.; Ferguson, M.A.
Phosphoglucomutase is absent in Trypanosoma brucei and redundantly substituted by phosphomannomutase and phospho-N-acetylglucosamine mutase
Mol. Microbiol.
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2012
Trypanosoma brucei (F4NCC2), Trypanosoma brucei, Trypanosoma brucei 427 (F4NCC2)
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Ji, T.; Zhang, C.; Zheng, L.; Dunaway-Mariano, D.; Allen, K.N.
Structural basis of the molecular switch between phosphatase and mutase functions of human phosphomannomutase 1 under ischemic conditions
Biochemistry
57
3480-3492
2018
Homo sapiens (O15305), Homo sapiens
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Andreotti, G.; Cabeza de Vaca, I.; Poziello, A.; Monti, M.C.; Guallar, V.; Cubellis, M.V.
Conformational response to ligand binding in phosphomannomutase2 insights into inborn glycosylation disorder
J. Biol. Chem.
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Homo sapiens (O15305), Homo sapiens
brenda
Oh, R.; Moon, S.; Cho, H.; Jang, W.; Kim, J.; Lee, J.; Kong, I.
Cloning and characterization of phosphomannomutase/phosphoglucomutase (pmm/pgm) gene of Vibrio anguillarum related to synthesis of LPS
Microbiol. Biotechnol. Lett.
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355-362
2016
Vibrio anguillarum, Vibrio anguillarum O1
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Kaur, T.; Ghosh, M.
Characterization and upregulation of bifunctional phosphoglucomutase/phosphomannomutase enzyme in an exobiopolymer overproducing strain of Acinetobacter haemolyticus
Microbiol. Res.
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Acinetobacter haemolyticus
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Andreotti, G.; Monti, M.C.; Citro, V.; Cubellis, M.V.
Heterodimerization of two pathological mutants enhances the activity of human phosphomannomutase2
PLoS ONE
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e0139882
2015
Homo sapiens (O15305), Homo sapiens
brenda
Citro, V.; Cimmaruta, C.; Liguori, L.; Viscido, G.; Cubellis, M.V.; Andreotti, G.
A mutant of phosphomannomutase1 retains full enzymatic activity, but is not activated by IMP Possible implications for the disease PMM2-CDG
PLoS ONE
12
e0189629
2017
Homo sapiens (O15305), Homo sapiens (Q92871), Homo sapiens
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He, C.; Zeng, S.; Teixeira da Silva, J.A.; Yu, Z.; Tan, J.; Duan, J.
Molecular cloning and functional analysis of the phosphomannomutase (PMM) gene from Dendrobium officinale and evidence for the involvement of an abiotic stress response during germination
Protoplasma
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1693-1704
2017
Dendrobium officinale (A0A0U1WZ18), Dendrobium officinale
brenda
Xu, J.; Sarma, A.V.S.; Wei, Y.; Beamer, L.J.; Van Doren, S.R.
Multiple ligand-bound states of a phosphohexomutase revealed by principal component analysis of NMR peak shifts
Sci. Rep.
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5343
2017
Pseudomonas aeruginosa (P26276)
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