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Literature summary for 2.7.7.3 extracted from

  • Izard, T.
    The crystal structures of phosphopantetheine adenylyltransferase with bound substrates reveal the enzyme's catalytic mechanism (2002), J. Mol. Biol., 315, 487-495.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
co-crystallization with pantetheine 4'-phosphate or ATP, space group: I23, with a dimer in the asymmetric unit, a solvent content of 57% and a volume-to-protein mass ratio of 288 A3 Da-1 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.007
-
3'-dephospho-CoA
-
Escherichia coli
0.022
-
diphosphate
-
Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6I6
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + pantetheine 4'-phosphate
-
Escherichia coli diphosphate + 3'-dephospho-CoA
-
r

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.9
-
-
Escherichia coli