On the action of pyrophosphate on 3-phosphoglyceraldehyde dehydrogenase.

On the Action of Pyrophosphate on 3-phospho- Glyceraldehyde

When pyrophosphate has been found to influence an enzymatic reaction, its action is usually indirect, that is as a chelator of free essential metal ions rather than directly on the protein catalyst. However, it appears that the latter situation holds for the action of pyrophosphate in the modification of reduced diphosphopyridine nucleotide’ to the product obtained by the action of 3-phosphogly...

The enzymatic significance of S-acetylation and N-acetylation of 3-phosphoglyceraldehyde dehydrogenase.

Studies on Es&e&?& coli Pyruvate Dehydrogenase Complex I. EFFECT OF BROMOPYRUVATE ON THE CATALYTIC ACTIVITIES OF THE COMPLEX*

Bromopyruvate inactivates the pyruvate dehydrogenase complex of Escherichia coli in a thiamine pyrophosphate (TPP)-dependent process. The catalytic activities of the individual enzyme components within the complex are not destroyed by bromopyruvate under similar conditions, but the activities of the pyruvate dehydrogenase and dihydrolipoyl dehydrogenase components are reduced in thiamine pyroph...

Interaction between adenine nucleotides and 3-phosphoglyceraldehyde dehydrogenase. I. Inhibition of the hydrolysis of S-acetyl-enzyme intermediate in the esterase activity.

The interaction of 3phosphoglyceraldehyde dehydrogenase with various adenine nucleotides has been studied in order to gain insight into the manner in which the coenzyme, NAD, is bound to the enzyme and how this binding affects the various catalytic activities of the protein. The effects of adenine nucleotides were examined on the enzymatic hydrolysis of p-nitrophenyl acetate. This reaction prov...

Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase.

The derivative of vitamin B1, thiamin pyrophosphate, is a cofactor of enzymes performing catalysis in pathways of energy production. In alpha2beta2-heterotetrameric human pyruvate dehydrogenase, this cofactor is used to cleave the Calpha-C(=O) bond of pyruvate followed by reductive acetyl transfer to lipoyl-dihydrolipoamide acetyltransferase. The dynamic nonequivalence of two, otherwise chemica...