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Literature summary for 6.3.2.5 extracted from

  • Kupke, T.
    Molecular Characterization of the 4'-Phosphopantothenoylcysteine Synthetase Domain of Bacterial Dfp Flavoproteins (2002), J. Biol. Chem., 277, 36137-36145.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
A275V unable to form dimers Escherichia coli
D203N unable to form dimers Escherichia coli
K289Q complete loss of enzymic activity Escherichia coli
N210D complete loss of enzymic activity, but intermediate 4’-phosphopanthotenoyl-CMP is formed Escherichia coli
T194V unable to form dimers Escherichia coli
T198V unable to form dimers Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
26100
-
2 * 26100, SDS-PAGE Escherichia coli
42000
-
gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine mechanism Escherichia coli

Subunits

Subunits Comment Organism
dimer 2 * 26100, SDS-PAGE Escherichia coli
More enzymic activity lies within the C-terminal domain of Dfp protein Escherichia coli