Design, synthesis and characterisation of a peptide with oxaloacetate decarboxylase activity

Taylor, Susan E., Rutherford, Trevor J. and Allemann, Rudolf Konrad ORCID: https://orcid.org/0000-0002-1323-8830 2001. Design, synthesis and characterisation of a peptide with oxaloacetate decarboxylase activity. Biorganic and Medicinal Chemistry Letters 11 (19) , pp. 2631-2635. 10.1016/S0960-894X(01)00519-4

Full text not available from this repository.

Abstract

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 μM, 100-fold lower than the previously described Oxaldie-2, which relied on aggregating α-helices for activity. Oxaldie-3 speeded decarboxylation by more than three orders of magnitude relative to simple amines. The 31-amino acid residue polypeptide Oxaldie-3 adopted a molten globule-like tertiary structure in solution and catalysed the decarboxylation of oxaloacetate with high specific activity. Its catalytic efficiency was increased by more than three orders of magnitude when compared to simple amines.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Chemistry Cardiff Catalysis Institute (CCI)
Subjects:	Q Science > QD Chemistry
Publisher:	Elsevier
ISSN:	0960-894X
Last Modified:	18 Oct 2022 13:19
URI:	https://orca.cardiff.ac.uk/id/eprint/13474

Citation Data

Cited 18 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item