Abstract
Pyruvate decarboxylase from Zymomonas mobilis is inhibited by 3-hydroxypyruvate, which can also act as a poor substrate. While catalysing the decarboxylation of this alternative substrate, the enzyme undergoes a progressive but partial inactivation over several hours. The extent of inactivation depends upon the pH and upon the concentration of 3-hydroxypyruvate. After partial inactivation and removal of unchanged 3-hydroxypyruvate, enzymic activity recovers slowly. We suggest that inactivation results from accumulation of enzyme-bound glycollaldehyde, which is relatively stable, possibly because it is dehydrated to form an acetyl group.
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- Apfel M. A., Ikeda B. H., Speckhard D. C., Frey P. A. Escherichia coli pyruvate dehydrogenase complex. Thiamin pyrophosphate-dependent inactivation by 3-bromopyruvate. J Biol Chem. 1984 Mar 10;259(5):2905–2909. [PubMed] [Google Scholar]
- Duggleby R. G. Regression analysis of nonlinear Arrhenius plots: an empirical model and a computer program. Comput Biol Med. 1984;14(4):447–455. doi: 10.1016/0010-4825(84)90045-3. [DOI] [PubMed] [Google Scholar]
- Kuo D. J., Dikdan G., Jordan F. Resolution of brewers' yeast pyruvate decarboxylase into two isozymes. J Biol Chem. 1986 Mar 5;261(7):3316–3319. [PubMed] [Google Scholar]
- Lowe P. N., Perham R. N. Bromopyruvate as an active-site-directed inhibitor of the pyruvate dehydrogenase multienzyme complex from Escherichia coli. Biochemistry. 1984 Jan 3;23(1):91–97. doi: 10.1021/bi00296a015. [DOI] [PubMed] [Google Scholar]
- Neale A. D., Scopes R. K., Wettenhall R. E., Hoogenraad N. J. Pyruvate decarboxylase of Zymomonas mobilis: isolation, properties, and genetic expression in Escherichia coli. J Bacteriol. 1987 Mar;169(3):1024–1028. doi: 10.1128/jb.169.3.1024-1028.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Uhlemann H., Schellenberger A. Glyoxylic acid as an active site marker of yeast pyruvate decarboxylase. FEBS Lett. 1976 Mar 15;63(1):37–39. doi: 10.1016/0014-5793(76)80189-5. [DOI] [PubMed] [Google Scholar]
- Ullrich J. Structure-function relationships in pyruvate decarboxylase of yeast and wheat germ. Ann N Y Acad Sci. 1982;378:287–305. doi: 10.1111/j.1749-6632.1982.tb31203.x. [DOI] [PubMed] [Google Scholar]
- Zehender H., Trescher D., Ullrich J. Improved purification of pyruvate decarboxylase from wheat germ. Its partial characterisation and comparison with the yeast enzyme. Eur J Biochem. 1987 Aug 17;167(1):149–154. doi: 10.1111/j.1432-1033.1987.tb13316.x. [DOI] [PubMed] [Google Scholar]