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The protective role of pyruvate against heat in activation of N ‐acetylneuraminate lyase
Author(s) -
Kolisis Fragiskos N.,
Sotiroudis Theodore G.,
Evangelopoulos Athanasios E.
Publication year - 1980
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(80)80362-0
Subject(s) - citation , foundation (evidence) , library science , political science , computer science , law
N-Acetylneuraminate lyase (EC 4.1.3 3) is the enzyme which catalyzes the reversible cleavage or synthesis of ~-acety~eumm~ic acid from pyruvate and N-acetyl-D-mannosamie [ 11. It is widely distributed in animal tissues and inbacteria [2]. It consists of 2 subunits with a monomer Mr -50 000 and it has 2 active sites~native enzyme molecule [3]. The enzyme from Clastidium perfkigeens belongs to the group of class I aldolases because it forms a Schiff base between the substrate pyruvate and a lysine residue of its active site in the course of the catalytic reaction [3-61. It is known that most enzymes are quickly inactivated above 55’C. However binding of small molecules or ions can alter s~i~c~tly the thermal stability of some proteins. A number of enzymes have been reported to be stable at high temperatures after interaction with substrates or coenzymes [7,8]. Here, we have studied the changes in the catalytic activity of ~~cetylneuraminate base as a function of temperature in presence or absence of its substrates. Our results indicate that N-acetylneuraminate lyase is effectively protected against heat inactivation by pyruvate. The protective effect of pyruvate can be used in a new simple step of the purification procedure of the enzyme.