2.7.7.3: pantetheine-phosphate adenylyltransferase
This is an abbreviated version!
For detailed information about pantetheine-phosphate adenylyltransferase, go to the full flat file.
Word Map on EC 2.7.7.3
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2.7.7.3
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ppats
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penultimate
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dpcoa
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pantothen
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pyrophosphate
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hexameric
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3\'-dephospho-coa
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nucleotidyltransferase
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dephosphocoenzyme
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phosphopantothenoylcysteine
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medicine
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drug development
- 2.7.7.3
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ppats
-
penultimate
-
dpcoa
-
pantothen
- pyrophosphate
-
hexameric
-
3\'-dephospho-coa
-
nucleotidyltransferase
-
dephosphocoenzyme
-
phosphopantothenoylcysteine
- medicine
- drug development
Reaction
Synonyms
3'-dephospho-CoA pyrophosphorylase, 4'-phosphopantetheine adenylyltransferase, 4-phosphopantetheine adenylyltransferase, CoaD, dephospho-CoA pyrophosphorylase, dephospho-coenzyme A pyrophosphorylase, Enterococcus faecalis PPAT, More, pantetheine phosphate adenylyltransferase, phosphopantetheine adenylyltransferase, PPAT
ECTree
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Engineering
Engineering on EC 2.7.7.3 - pantetheine-phosphate adenylyltransferase
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I4V/N76Y
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the mutant is a homotetramer. Despite structural differences between wild type enzyme and IV4/N76Y, they have similar ligand-binding properties
R90A/D94A
N106H
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the enzyme mutant is less sensitive to inhibition by compound D compared to the wild-type enzyme
N106Y
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the enzyme mutant is less sensitive to inhibition by compound D compared to the wild-type enzyme
V136F
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the enzyme mutant is less sensitive to inhibition by compound D compared to the wild-type enzyme
N106H
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the enzyme mutant is less sensitive to inhibition by compound D compared to the wild-type enzyme
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N106Y
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the enzyme mutant is less sensitive to inhibition by compound D compared to the wild-type enzyme
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V136F
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the enzyme mutant is less sensitive to inhibition by compound D compared to the wild-type enzyme
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F8L
the enzyme mutant is less sensitive to inhibition by compound D compared to the wild-type enzyme
N107H
the enzyme mutant is less sensitive to inhibition by compound D compared to the wild-type enzyme
T117N
the enzyme mutant is less sensitive to inhibition by compound D compared to the wild-type enzyme
in silico mutation, ligand acetyl-CoA fails to maintain its position inside the binding cavity
R90A/D94A
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in silico mutation, ligand acetyl-CoA fails to maintain its position inside the binding cavity
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