Kinetic mechanism of pyruvate decarboxylase. Evidence for a specific protonation of the enzymic intermediate.

Abstract:

:Decarboxylation of pyruvate by pyruvate decarboxylase (EC 4.1.1.1) was performed in a reaction mixture containing 50% deuterium. The isolated product, acetaldehyde, was investigated directly by 1H NMR and by mass spectrometry after conversion to the 2,4-dinitrophenyl hydrazone. The protium content of 56% at acetaldehyde C1 demonstrates a specific protonation of the corresponding intermediate by the enzyme. Proton inventory studies and enzyme modification indicate the 4' amino group of the coenzyme, thiamine pyrophosphate, in an immonium structure being a possible proton donor. A 'partially concerted' mechanism is suggested for the reaction steps following the decarboxylation.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Ermer J,Schellenberger A,Hübner G

doi

10.1016/0014-5793(92)80238-c

keywords:

subject

Has Abstract

pub_date

1992-03-09 00:00:00

pages

163-5

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(92)80238-C

journal_volume

299

pub_type

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