Disease relevance of Pyruvoyl Group

• A covalently linked pyruvoyl group is essential for the enzymatic activity of S-adenosylmethionine decarboxylase from Escherichia coli [1].
• Identification of D-proline reductase from Clostridium sticklandii as a selenoenzyme and indications for a catalytically active pyruvoyl group derived from a cysteine residue by cleavage of a proprotein [2].

High impact information on Pyruvoyl Group

• The pyruvoyl group serves as the prosthetic group for the decarboxylation reaction [3].
• Pyruvamide semicarbazone formation. Kinetics, mechanism, and pertinence to pyruvamide-dependent histidine decarboxylase [4].
• The changes of the scattering pattern upon binding of the substrate-like activator pyruvamide indicate that the structure expands in the course of the enzyme activation [5].
• Cys242, as the precursor of the pyruvoyl group in GrdE, was changed to alanine, serine, or threonine by site-directed mutagenesis [6].
• In the closed enzyme subunit, one molecule of pyruvamide is bound in the active site channel, and is located in the vicinity of the thiazolium ring of the cofactor [7].

Associations of Pyruvoyl Group with other chemical compounds

• The crystal structure of the complex of the thiamine diphosphate dependent tetrameric enzyme pyruvate decarboxylase (PDC) from brewer's yeast strain with the activator pyruvamide has been determined to 2.4 A resolution [7].

References