3.6.1.42: guanosine-diphosphatase
This is an abbreviated version!
For detailed information about guanosine-diphosphatase, go to the full flat file.
Word Map on EC 3.6.1.42
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3.6.1.42
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charcot-marie-tooth
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neuropathy
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demyelinate
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nerve
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ganglioside-induced
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purinergic
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differentiation-associated
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ectonucleotidases
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gdpase
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apyrase
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ecto-5\'-nucleotidase
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sural
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ectonucleoside
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ntpdase3
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sh3tc2
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ecto-enzymes
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ecto-adenosine
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3.6.1.5
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ecto-ntpdase
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charcot
- 3.6.1.42
- charcot-marie-tooth
- neuropathy
-
demyelinate
- nerve
-
ganglioside-induced
-
purinergic
-
differentiation-associated
- ectonucleotidases
- gdpase
- apyrase
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ecto-5\'-nucleotidase
-
sural
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ectonucleoside
- ntpdase3
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sh3tc2
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ecto-enzymes
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ecto-adenosine
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3.6.1.5
- ecto-ntpdase
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charcot
Reaction
Synonyms
APY1, DIPP1, E-NTPDase, ecto-nucleoside triphosphate diphosphohydrolase, gda1p (GDA1 gene product), Gdap1, Gdp1p, GDPase, guanosine diphosphatase, KlGdap1, phosphatase, guanosine di-, UDPase
ECTree
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Engineering
Engineering on EC 3.6.1.42 - guanosine-diphosphatase
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additional information
disruption of gene gda1 leads to a mutant with 90% reduced GDP hydrolysis activity compared to the wild-type, the mutant also shows severely impaired O-mannosylation and reduced cell wall phosphate content and other phenotypes, but the formation of hyphae is uneffected, overview
additional information
enzyme null mutants show 95% reduced activity in vitro and inhibition of glycosyltransferases utilizing uridine and guanosine nucleotide sugars due to accumulation of nucleoside diphosphates, the transport of both GDP-mannose and UDP-GlcNAc into the Golgi lumen is reduced in the null mutants, complementation of the disruption mutant by recombinant expression of the wild-type enzyme or the Saccharomyces cerevisiae enzyme
additional information
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enzyme null mutants show 95% reduced activity in vitro and inhibition of glycosyltransferases utilizing uridine and guanosine nucleotide sugars due to accumulation of nucleoside diphosphates, the transport of both GDP-mannose and UDP-GlcNAc into the Golgi lumen is reduced in the null mutants, complementation of the disruption mutant by recombinant expression of the wild-type enzyme or the Saccharomyces cerevisiae enzyme
additional information
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construction of s disruption mutant showing defects in N-glycosylation of other proteins