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2-deoxyribose 1-phosphate
2-deoxyribose 5-phosphate
-
-
-
?
3-phospho-D-glyceric acid
?
-
no mutase activity
-
?
alpha-D-glucose 1,6-bisphosphate + H2O
alpha-D-glucose 6-phosphate + phosphate
alpha-D-glucose 1-phosphate
?
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
alpha-D-glucose 6-phosphate
alpha-D-glucose 1-phosphate
23% of the activity with alpha-D-glucose 1-phosphate
-
r
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
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 1,6-diphosphate
?
D-glucose 1-phosphate + D-fructose 1,6-diphosphate
D-glucose 1,6-diphosphate + D-fructose 1-phosphate + D-fructose 6-phosphate
-
synthesis of glucose 1,6-diphosphate is an additional activity
synthesis of glucose 1,6-diphosphate is an additional activity
?
D-glucose 6-phosphate
alpha-D-glucose 1-phosphate
D-glucose-1-phosphate
D-glucose-6-phosphate
D-glucose-1-phosphate
glucose-6-phosphate
D-Mannose 1-phosphate
D-Mannose 6-phosphate
-
-
-
?
D-mannose-1-phosphate
D-mannose-6-phosphate
Glucose 1-phosphate + 1,3-bisphosphoglycerate
Glucose 1,6-diphosphate + glycerate 3-phosphate
-
synthesis of glucose 1,6-diphosphate is an additional activity
synthesis of glucose 1,6-diphosphate is an additional activity
?
Glucose 6-phosphate
Glucose 1-phosphate
Mannose 1-phosphate
?
-
-
-
?
N-acetyl-D-glucosamine-1-phosphate
N-acetyl-D-glucosamine-6-phosphate
-
no mutase activity
-
?
additional information
?
-
alpha-D-glucose 1,6-bisphosphate + H2O

alpha-D-glucose 6-phosphate + phosphate
-
-
-
?
alpha-D-glucose 1,6-bisphosphate + H2O
alpha-D-glucose 6-phosphate + phosphate
-
-
-
?
alpha-D-glucose 1-phosphate

?
-
glucosylation of teichoic acid
-
?
alpha-D-glucose 1-phosphate
?
-
key enzyme in carbohydrate metabolism
-
?
alpha-D-glucose 1-phosphate
?
-
degradation of lactose in lactic acid bacteria
-
?
alpha-D-glucose 1-phosphate
?
-
degradation of sucrose in plants
-
?
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
alpha-D-glucose 6-phosphate
-
-
-
?
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
alpha-D-glucose 6-phosphate
-
-
-
?
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
Cassia corymbosa
-
-
-
?
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
alpha-D-glucose 6-phosphate
-
-
-
?
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
alpha-D-glucose 6-phosphate
-
the beta-form is inactive
-
?
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
enzyme is highly specific for substrate and product
-
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
alpha-D-glucose 6-phosphate
-
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
the forward reaction is faster than the reverse reaction
-
?
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
-
the beta-form is inactive
-
?
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
-
-
-
?
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
-
-
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
alpha-D-glucose 6-phosphate
-
-
-
?
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
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
SP-1 shows preference for glucose-1-phosphate rather than mannose-1-phosphate
-
?
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
SP-1 shows preference for glucose-1-phosphate rather than mannose-1-phosphate
-
?
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
alpha-D-glucose 6-phosphate
-
-
?
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
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
-
-
r
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-glucose 1-phosphate
D-glucose 6-phosphate
Cassia corymbosa
-
-
-
?
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
-
-
-
?
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-glucose 1-phosphate
D-glucose 6-phosphate
-
-
r
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-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
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-glucose 1-phosphate
D-glucose 6-phosphate
the enzyme also catalyzes the interconversion of alpha-D-mannose 1-phosphate and D-mannose 6-phosphate
-
r
alpha-D-glucose 1-phosphate
D-glucose 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-glucose 1-phosphate
D-glucose 6-phosphate
the enzyme also catalyzes the interconversion of alpha-D-mannose 1-phosphate and D-mannose 6-phosphate
-
r
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
-
-
?
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
-
-
-
r
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
-
-
-
r
alpha-D-mannose 1-phosphate

D-mannose-6-phosphate
SP-1 shows preference for glucose-1-phosphate rather than mannose-1-phosphate
-
?
alpha-D-mannose 1-phosphate
D-mannose-6-phosphate
SP-1 shows preference for glucose-1-phosphate rather than mannose-1-phosphate
-
?
D-glucose 1,6-diphosphate

?
-
-
-
?
D-glucose 1,6-diphosphate
?
-
-
-
?
D-glucose 6-phosphate

alpha-D-glucose 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-glucose 6-phosphate
alpha-D-glucose 1-phosphate
the enzyme also catalyzes the interconversion of alpha-D-mannose 1-phosphate and D-mannose 6-phosphate. No activity toward glucosamine 6-phosphate or N-acetylglucosamine 6-phosphate
-
r
D-glucose 6-phosphate
alpha-D-glucose 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-glucose 6-phosphate
alpha-D-glucose 1-phosphate
the enzyme also catalyzes the interconversion of alpha-D-mannose 1-phosphate and D-mannose 6-phosphate. No activity toward glucosamine 6-phosphate or N-acetylglucosamine 6-phosphate
-
r
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-glucose-1-phosphate

glucose-6-phosphate
-
-
-
?
D-glucose-1-phosphate
glucose-6-phosphate
-
-
-
?
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 6-phosphate

?
-
glucosylation of teichoic acid
-
?
Glucose 6-phosphate
?
-
synthesis of glucose 1-phosphate for the formation of UDPglucose
-
?
Glucose 6-phosphate

Glucose 1-phosphate
-
-
-
?
Glucose 6-phosphate
Glucose 1-phosphate
-
-
-
?
Glucose 6-phosphate
Glucose 1-phosphate
-
-
-
?
additional information

?
-
-
isozyme PGM2 also displays activities of phosphoribomutase and glucose 1,6-bisphosphate synthase
-
?
additional information
?
-
-
isozyme PGM2 also displays activities of phosphoribomutase and glucose 1,6-bisphosphate synthase
-
?
additional information
?
-
-
PGM from Clostridium thermocellum is a dual-specificity enzyme with phosphoglucomutase and phosphomannomutase activities
-
?
additional information
?
-
no substrate: alpha-D-mannose 1-phosphate, beta-D-glucose 1-phosphate
-
?
additional information
?
-
-
no substrate: alpha-D-mannose 1-phosphate, beta-D-glucose 1-phosphate
-
?
additional information
?
-
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities
-
?
additional information
?
-
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities. Strongly conserved residue His329 in the active site is critical for enzyme activity. His329 is appropriately positioned to abstract a proton from the O1/O6 hydroxyl of the phosphosugar substrates, and thus may serve as the general base in the reaction
-
?
additional information
?
-
-
no activity with alpha-D-ribose 5-phosphate
-
?
additional information
?
-
-
Pgm3 functions as the major phosphoribomutase in vivo
-
?
additional information
?
-
-
phosphoglucomutases Pgm1, Pgm2, and Pgm3, EC 5.4.2.2, of Saccharomyces cerevisiae show ability to interconvert ribose-1-phosphate and ribose-5-phosphate. The purified proteins, studied in vitro with regard to their kinetic properties on glucose-1-phosphate and ribose-1-phosphate, are all active on both substrates with Pgm1 exhibiting only residual activity on ribose-1-phosphate. The Pgm2 and Pgm3 proteins have almost equal kinetic properties on ribose-1-phosphate, but Pgm2 has a 2000times higher preference for glucose-1-phosphate when compared to Pgm3
-
?
additional information
?
-
-
no activity with alpha-D-ribose 5-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
?
-
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
-
?
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 1-phosphate
alpha-D-glucose 6-phosphate
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
-
-
-
-
?
D-glucose 6-phosphate
alpha-D-glucose 1-phosphate
additional information
?
-
alpha-D-glucose 1-phosphate

?
-
glucosylation of teichoic acid
-
-
?
alpha-D-glucose 1-phosphate
?
-
key enzyme in carbohydrate metabolism
-
-
?
alpha-D-glucose 1-phosphate
?
-
degradation of lactose in lactic acid bacteria
-
-
?
alpha-D-glucose 1-phosphate
?
-
degradation of sucrose in plants
-
-
?
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
-
-
-
r
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
-
-
r
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-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
-
-
-
?
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
-
-
-
r
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
-
-
-
-
r
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
-
-
-
-
?
alpha-D-glucose 1-phosphate
D-glucose 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-glucose 1-phosphate
D-glucose 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-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
-
-
-
?
D-glucose 6-phosphate

alpha-D-glucose 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-glucose 6-phosphate
alpha-D-glucose 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
Glucose 6-phosphate

?
-
glucosylation of teichoic acid
-
-
?
Glucose 6-phosphate
?
-
synthesis of glucose 1-phosphate for the formation of UDPglucose
-
-
?
additional information

?
-
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities
-
-
?
additional information
?
-
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities. Strongly conserved residue His329 in the active site is critical for enzyme activity. His329 is appropriately positioned to abstract a proton from the O1/O6 hydroxyl of the phosphosugar substrates, and thus may serve as the general base in the reaction
-
-
?
additional information
?
-
-
Pgm3 functions as the major phosphoribomutase in vivo
-
-
?
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
-
-
?
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alpha-D-Glucose 1,6-bisphosphate
alpha-D-glucose 1,6-diphosphate
D-fructose-6-phosphate
-
-
D-glucose-1,6-bisphosphate
glucose 1,6-bisphosphate
absolutely required
Imidazol
-
addition at concentrations below that of Mg2+ increases the activity
alpha-D-Glucose 1,6-bisphosphate

-
dependent on
alpha-D-Glucose 1,6-bisphosphate
dependent on
alpha-D-Glucose 1,6-bisphosphate
dependent on
alpha-D-Glucose 1,6-bisphosphate
dependent on
alpha-D-Glucose 1,6-bisphosphate
-
dependent on
alpha-D-Glucose 1,6-bisphosphate
dependent on
alpha-D-Glucose 1,6-bisphosphate
-
dependent on
alpha-D-Glucose 1,6-bisphosphate
2fold increase of activity at 0.0001 mM
alpha-D-Glucose 1,6-bisphosphate
-
dependent on
alpha-D-Glucose 1,6-bisphosphate
-
dependent on
alpha-D-Glucose 1,6-bisphosphate
the maximum activity is obtained in the presence of more than 0.2 mM alpha-D-glucose 1,6-bisphosphate
alpha-D-Glucose 1,6-bisphosphate
dependent on
alpha-D-glucose 1,6-diphosphate

-
-
alpha-D-glucose 1,6-diphosphate
-
Km: 0.00053 mM phosphoglucomutase I, 0.00232 mM, phosphoglucomutase II
alpha-D-glucose 1,6-diphosphate
-
-
alpha-D-glucose 1,6-diphosphate
Cassia corymbosa
-
Km: 0.0005 mM
alpha-D-glucose 1,6-diphosphate
-
Km: 0.00077-0.00163 mM
alpha-D-glucose 1,6-diphosphate
-
Km: 0.0002 mM
alpha-D-glucose 1,6-diphosphate
-
required
alpha-D-glucose 1,6-diphosphate
-
the beta-form is inactive
alpha-D-glucose 1,6-diphosphate
-
-
alpha-D-glucose 1,6-diphosphate
-
Km: 0.00145 mM
alpha-D-glucose 1,6-diphosphate
-
-
alpha-D-glucose 1,6-diphosphate
-
Km: 0.00224 mM
alpha-D-glucose 1,6-diphosphate
-
peak I enzyme Km: 0.0018 mM
alpha-D-glucose 1,6-diphosphate
-
peak II enzyme, Km: 0.0022 mM
alpha-D-glucose 1,6-diphosphate
-
-
cysteine

-
required
cysteine
-
2 mM required, can be substituted by EDTA
D-glucose-1,6-bisphosphate

-
-
D-glucose-1,6-bisphosphate
-
-
D-glucose-1,6-bisphosphate
-
EDTA

-
activation
EDTA
-
2 mM required, can be substituted by cysteine
EDTA
-
addition at concentrations below that of Mg2+ increases the activity
histidine

-
required
histidine
-
pH-titration studies of His residues
additional information

-
high pullulan yield is related to high activities of alpha-phosphoglucose mutase
-
additional information
-
pH-titration studies of serine phosphate
-
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3.5
2-deoxyribose-1-phosphate
-
90°C
0.016 - 0.033
alpha-D-Glucose 1,6-bisphosphate
0.000582 - 3.53
alpha-D-glucose 1-phosphate
0.4392 - 1.15
alpha-D-mannose 1-phosphate
0.00103
D-glucose 1,6-diphosphate
-
in 41 mM 1,3-diaza-2,4-cyclopentadiene /HCl (pH 7.6), 5 mM MgCl2, at 25°C
2 - 13
D-glucose 6-phosphate
0.0952 - 3
D-glucose-1-phosphate
0.02
D-mannose 1-phosphate
-
25°C, pH 7.6
0.0915 - 3.2
D-mannose-1-phosphate
0.022
glucose 1-phosphate
-
-
0.017
mannose 1-phosphate
-
-
additional information
additional information
-
0.016
alpha-D-Glucose 1,6-bisphosphate

-
25°C, pH 7.6
0.033
alpha-D-Glucose 1,6-bisphosphate
-
-
0.000582
alpha-D-glucose 1-phosphate

pH and temperature not specified in the publication
0.0013
alpha-D-glucose 1-phosphate
H308N/H329N double mutant
0.0013
alpha-D-glucose 1-phosphate
S108A mutant
0.0024
alpha-D-glucose 1-phosphate
S108A/H308N double mutant
0.0027
alpha-D-glucose 1-phosphate
K118L/H109Q double mutant
0.0028
alpha-D-glucose 1-phosphate
R20A mutant
0.003
alpha-D-glucose 1-phosphate
-
PGM2, in 50 mM HEPES, pH 7.1, 5 mM MgCl2, at 30°C
0.0034
alpha-D-glucose 1-phosphate
S108D mutant
0.008
alpha-D-glucose 1-phosphate
H109Q mutant
0.008
alpha-D-glucose 1-phosphate
K118L mutant
0.0082
alpha-D-glucose 1-phosphate
-
PGM1, in 50 mM HEPES, pH 7.1, 5 mM MgCl2, at 30°C
0.009
alpha-D-glucose 1-phosphate
R247A mutant
0.01
alpha-D-glucose 1-phosphate
H308N mutant
0.01
alpha-D-glucose 1-phosphate
S108V mutant
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
0.016
alpha-D-glucose 1-phosphate
H329N mutant
0.0168
alpha-D-glucose 1-phosphate
pH 7.2, 30°C
0.018
alpha-D-glucose 1-phosphate
-
-
0.0195
alpha-D-glucose 1-phosphate
-
mutant R247A
0.02
alpha-D-glucose 1-phosphate
-
25°C, pH 7.6
0.02135
alpha-D-glucose 1-phosphate
pH and temperature not specified in the publication
0.023
alpha-D-glucose 1-phosphate
-
-
0.026
alpha-D-glucose 1-phosphate
-
recombinant His-tagged Pgm2, pH 7.5, 30°C
0.0273
alpha-D-glucose 1-phosphate
-
wild-type
0.0279
alpha-D-glucose 1-phosphate
-
mutant R421C
0.03
alpha-D-glucose 1-phosphate
-
mutant H329A, pH 7.5, temperature not specified in the publication
0.057 - 0.062
alpha-D-glucose 1-phosphate
-
isozyme PGM2
0.06
alpha-D-glucose 1-phosphate
-
peak I enzyme
0.06
alpha-D-glucose 1-phosphate
-
recombinant His-tagged Pgm1, pH 7.5, 30°C
0.065
alpha-D-glucose 1-phosphate
Cassia corymbosa
-
-
0.08
alpha-D-glucose 1-phosphate
-
wild-type enzyme, pH 7.5, temperature not specified in the publication
0.08
alpha-D-glucose 1-phosphate
-
at pH 7.0 and 30°C
0.0805 - 0.088
alpha-D-glucose 1-phosphate
-
isozyme PGM1
0.1
alpha-D-glucose 1-phosphate
-
in 41 mM 1,3-diaza-2,4-cyclopentadiene /HCl (pH 7.6), 5 mM MgCl2, at 25°C
0.1 - 2
alpha-D-glucose 1-phosphate
recombinant enzyme, pH 7.4, 30°C
0.112
alpha-D-glucose 1-phosphate
-
recombinant His-tagged Pgm3, pH 7.5, 30°C
0.12
alpha-D-glucose 1-phosphate
-
peak II enzyme
0.19
alpha-D-glucose 1-phosphate
isozyme PGM-I, in 50 mM HEPES-KOH, pH 8.0, at 37°C
0.2 - 1
alpha-D-glucose 1-phosphate
recombinant His-tagged enzyme, pH 7.6, temperature not specified in the publication
0.2228
alpha-D-glucose 1-phosphate
SP-1, in 50 mM Tris-HCl (pH 7.5), at 37°C
0.36
alpha-D-glucose 1-phosphate
-
-
0.41
alpha-D-glucose 1-phosphate
-
recombinant wild type enzyme, at 60°C
0.65
alpha-D-glucose 1-phosphate
at pH and °C
2
alpha-D-glucose 1-phosphate
-
purified recombinant enzyme
2.6
alpha-D-glucose 1-phosphate
-
-
3.53
alpha-D-glucose 1-phosphate
isozyme PGM-II, in 50 mM HEPES-KOH, pH 8.0, at 37°C
0.4392
alpha-D-mannose 1-phosphate

SP-1, in 50 mM Tris-HCl (pH 7.5), at 37°C
0.44
alpha-D-mannose 1-phosphate
-
recombinant wild type enzyme, at 60°C
1.15
alpha-D-mannose 1-phosphate
-
at pH 7.5 and 30°C
2
D-glucose 6-phosphate

pH 6.5, 65°C, mutant enzyme S309D
6
D-glucose 6-phosphate
pH 6.5, 65°C, mutant enzyme S309Q
8
D-glucose 6-phosphate
pH 6.5, 65°C, mutant enzyme S309N
8
D-glucose 6-phosphate
pH 6.5, 65°C, mutant enzyme S309T
9
D-glucose 6-phosphate
pH 6.5, 65°C, mutant enzyme S309A
12
D-glucose 6-phosphate
pH 6.5, 65°C, mutant enzyme S309V
13
D-glucose 6-phosphate
pH 6.5, 65°C, wild-type enzyme
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
0.0915
D-mannose-1-phosphate

-
isoenzyme PH0923, 37°C
3.2
D-mannose-1-phosphate
-
90°C
additional information
additional information

-
kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
KM mannose-1-phosphate isoenzyme PH0923S101A not detectable, 37°C
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics of wild-type and mutant H329A enzymes, overview
-
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evolution
-
the enzyme belongs to the alpha-D-phosphohexomutase enzyme superfamily
malfunction

-
targeted deletion of pgmA in Yersinia pestis strain KIM5 results in loss of autoaggregation, the deletion mutant displays more than 1000fold increased sensitivity to polymyxin B compared to the parental strain
malfunction
the pgm deletion mutant has impaired growth in vitro, is deficient in the ability to utilize alpha-D-galactose as a carbon source and displays reduced O-antigen polymer length
malfunction
-
whereas pgm2 and pgm3 single mutants are undistinguishable from the wild type, loss of both PGM2 and PGM3 severely impairs male and female gametophyte function. Double mutant pollen completes development but fails to germinate, double mutant ovules also develop normally, but approximately half remain unfertilized 2 d after pollination
malfunction
-
only mutants with a deletion of PGM3, not of PGM1 or PGM2, hyperaccumulate ribose-1-phosphate
malfunction
-
an enzyme-deficient mutant shows significantly reduced survival in embryonic trophoblast cells and in mice, and induces high protective immunity in BALB/c mice. Moreover, the mutant elicits an anti-Brucella-specific immunoglobulin G response and induces the secretion of gamma interferon and interleukin-2
malfunction
-
complete enzyme loss results in dwarf growth, prematurely die off, and inability to develop a functional inflorescence
malfunction
enzyme depletion is associated with declined cellular glycogen content and decreased rates of glycogenolysis and glycogenesis. Furthermore, enzyme depletion suppresses cell proliferation under long-term repetitive glucose depletion
malfunction
-
enzyme loss causes male sterility
malfunction
-
whereas pgm2 and pgm3 single mutants are undistinguishable from the wild type, loss of both PGM2 and PGM3 severely impairs male and female gametophyte function. Double mutant pollen completes development but fails to germinate, double mutant ovules also develop normally, but approximately half remain unfertilized 2 d after pollination
malfunction
-
an enzyme-deficient mutant shows significantly reduced survival in embryonic trophoblast cells and in mice, and induces high protective immunity in BALB/c mice. Moreover, the mutant elicits an anti-Brucella-specific immunoglobulin G response and induces the secretion of gamma interferon and interleukin-2
malfunction
-
targeted deletion of pgmA in Yersinia pestis strain KIM5 results in loss of autoaggregation, the deletion mutant displays more than 1000fold increased sensitivity to polymyxin B compared to the parental strain
malfunction
-
the pgm deletion mutant has impaired growth in vitro, is deficient in the ability to utilize alpha-D-galactose as a carbon source and displays reduced O-antigen polymer length
metabolism

-
cytosolic PGM activity is not limiting for carbon metabolism
metabolism
-
PGM is a key enzyme in carbohydrate metabolism, where it catalyzes the reversible transfer of a phosphate group between C-1 and C-6 of D-glucose via D-glucose 1,6-diphosphate
metabolism
-
PGM is a key enzyme in carbohydrate metabolism, where it catalyzes the reversible transfer of a phosphate group between C-1 and C-6 of D-glucose via D-glucose 1,6-diphosphate
metabolism
-
cytosolic PGM activity is not limiting for carbon metabolism
physiological function

Pgm is required by Salmonella enterica serovar Typhimurium for O-antigen production, resistance to antimicrobial peptides, and in vivo fitness
physiological function
-
PgmA is required for efficient autoaggregation in Yersinia pestis and plays an important role in antimicrobial peptide resistance
physiological function
-
overexpression of pgm gene has no significant effect on UDP-glucose and UDP-galactose levels and increased alpha-Pgm activity does not significantly change the lactate production
physiological function
-
pollen germination requires cytosolic PGM activity
physiological function
Unlike the majority of alpha-phosphoglucomutases, the described enzyme of 252 residues with alpha-phosphoglucomutase activity, is related to eukaryotic phosphomannomutases and belongs to HAD-superfamily hydrolase, subfamily IIB.
physiological function
-
the enzyme catalyzes an intramolecular phosphoryl transfer across its phosphosugar substrates, which are precursors in the synthesis of exoproducts involved in bacterial virulence
physiological function
the enzyme is involved in biosynthesis of sphingans, extracellular polysaccharides
physiological function
-
the enzyme is involved in glycogen catabolism
physiological function
the enzyme plays an important role in polysaccharide capsule formation and virulence in a number of bacterial pathogens
physiological function
-
the plastidial PGM limits photosynthetic carbon flow into starch
physiological function
-
the enzyme is essential for glucose phosphate partitioning and, therefore, for syntheses of sucrose and cell wall components
physiological function
the enzyme is necessary for sustained cell growth under repetitive glucose depletion
physiological function
the enzyme is required for hyphal growth, polysaccharide production, and cell wall integrity
physiological function
-
pollen germination requires cytosolic PGM activity
physiological function
-
the enzyme is required for hyphal growth, polysaccharide production, and cell wall integrity
physiological function
-
PgmA is required for efficient autoaggregation in Yersinia pestis and plays an important role in antimicrobial peptide resistance
physiological function
-
Pgm is required by Salmonella enterica serovar Typhimurium for O-antigen production, resistance to antimicrobial peptides, and in vivo fitness
physiological function
-
the enzyme plays an important role in polysaccharide capsule formation and virulence in a number of bacterial pathogens
physiological function
-
the enzyme is involved in biosynthesis of sphingans, extracellular polysaccharides
additional information

-
analysis of conformational flexibility of different forms of phosphoglucomutase/phosphomannomutase in solution, including its active, phosphorylated state and the unphosphorylated state that occurs transiently during the catalytic cycle, by hydrogen-deuterium exchange by mass spectrometry and small angle x-ray scattering. Both ligand binding and phosphorylation of the catalytic phosphoserine affect the overall flexibility of the enzyme in solution
additional information
structure homology modeling, overview
additional information
-
structure homology modeling, overview
additional information
-
structure homology modeling, overview
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