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diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-alpha-D-mannose
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-D-mannose
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GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
additional information
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diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
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diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
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diphosphate + GDP-mannose
GTP + alpha-D-mannose 1-phosphate
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GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-alpha-D-mannose
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r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-alpha-D-mannose
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GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
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r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
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GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
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r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
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GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
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GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
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r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
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?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
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GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
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GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
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?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
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?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
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r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
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regulation of the enzyme expression, overview
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r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
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r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
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regulation of the enzyme expression, overview
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r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
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GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
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?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
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?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
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?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
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?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
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?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
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?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
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r
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
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r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
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r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
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r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
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r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
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r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
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enzyme regulates GDP-D-mannose synthesis through feedback inhibition
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r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
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r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
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?
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
enzyme of alginate biosynthetic pathway
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r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
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r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
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?
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
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r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
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?
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
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r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
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r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
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r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
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r
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
overexpression leads to an increase in cellular GDPmannose levels
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GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
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r
additional information
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repression of GMPP in yeast leads to phenotypes including hyphal lysis, defective cell wall, and failure of polarized growth and branching site selection, and cell separation
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additional information
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repression of GMPP in yeast leads to phenotypes including hyphal lysis, defective cell wall, and failure of polarized growth and branching site selection, and cell separation
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additional information
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repression of GMPP in yeast leads to phenotypes including hyphal lysis, defective cell wall, and failure of polarized growth and branching site selection, and cell separation
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additional information
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the enzyme of Burkholderia cenocepacia, encoded by gene bceA, is bifunctional exhibiting phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities
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additional information
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the enzyme of Burkholderia cepacia, encoded by gene bceA, is bifunctional exhibiting phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities
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additional information
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the enzyme of Burkholderia cepacia, encoded by gene bceA, is bifunctional exhibiting phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities
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?
additional information
?
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the enzyme of Burkholderia cepacia, encoded by gene bceA, is bifunctional exhibiting phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities
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?
additional information
?
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the enzyme of Burkholderia cepacia, encoded by gene bceA, is bifunctional exhibiting phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities
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additional information
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truncated GDP-mannose pyrophosphorylase domain of the whole length enzyme shows almost 100fold less sugar nucleotidyltransferase activity with only GTP and mannose 1-phosphate as substrates. The enzyme accepts all five naturally occurring NTPs (ATP, CTP, GTP, dTTP and UTP) and a range of sugar-1-phosphates (glucose-, mannose-, galactose-, glucosamine-, N-acetylglucosamine- and fucose-1-phosphate)
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additional information
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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
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additional information
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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
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additional information
?
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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
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