Design, synthesis and characterisation of a peptide with oxaloacetate decarboxylase activity.
The synthesis of Oxaldie-3, a synthetic 31-residue peptide with oxaloacetate decarboxylase activity, is described. Biophysical characterisation by gel filtration, CD and NMR spectroscopy indicated that the peptide adopted a folded structure in solution. Oxaldie-3 was an efficient catalyst at concentrations as low as 2 microM, 100-fold lower than the previously described Oxaldie-2, which relied on aggregating alpha-helices for activity. Oxaldie-3 speeded decarboxylation by more than three orders of magnitude relative to simple amines.
Taylor
S E
SE
The University of Birmingham, School of Chemistry, Edgbaston, Birmingham B15 2TT, UK.
Rutherford
T J
TJ
Allemann
R K
RK
D000595:Amino Acid Sequence; D002262:Carboxy-Lyases / Q000737:chemistry / Q000378:metabolism*; D002384:Catalysis; D002942:Circular Dichroism; D007700:Kinetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
D009842:Oligopeptides; D010455:Peptides; C439168:oxaldie-3; D002262:Carboxy-Lyases; C021916:oxaloacetate decarboxylase