Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

Reaction

ATP
+
pantetheine 4'-phosphate
=
diphosphate
+
3'-dephospho-CoA

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

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.3 pantetheine-phosphate adenylyltransferase

Engineering

Engineering on EC 2.7.7.3 - pantetheine-phosphate adenylyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R106A
-
pantothenate kinase (PanK) mutant
I4V/N76Y
-
the mutant is a homotetramer. Despite structural differences between wild type enzyme and IV4/N76Y, they have similar ligand-binding properties
R90A/D94A
N106H
-
the enzyme mutant is less sensitive to inhibition by compound D compared to the wild-type enzyme
N106Y
-
the enzyme mutant is less sensitive to inhibition by compound D compared to the wild-type enzyme
V136F
-
the enzyme mutant is less sensitive to inhibition by compound D compared to the wild-type enzyme
N106H
-
the enzyme mutant is less sensitive to inhibition by compound D compared to the wild-type enzyme
-
N106Y
-
the enzyme mutant is less sensitive to inhibition by compound D compared to the wild-type enzyme
-
V136F
-
the enzyme mutant is less sensitive to inhibition by compound D compared to the wild-type enzyme
-
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