24. Ulusal Biyokimya Kongresi - Türk Biyokimya Dergisi

XXIV. ULUSAL B‹YOK‹MYA KONGRES‹
25 - 28 Eylül 2012
Dedeman Otel - Konya
24. Ulusal Biyokimya Kongresi, Konya [24 th National Biochemistry Congress, Konya / TURKEY]
İÇİNDEKİLER
P089 - ZINC ION; INHIBITOR OR ACTIVATOR OF HUMAN
FRUCTOSE 1,6 BISPHOSPHATE ALDOLASE
Neşe HAYAT AKSOY
AKSARAY ÜNİVERSİTESİ, Saglık YO, AKSARAY
P089 - ZINC ION; INHIBITOR OR ACTIVATOR OF HUMAN
FRUCTOSE 1,6 BISPHOSPHATE ALDOLASE
Neşe HAYAT AKSOY
School of Health, AKSARAY
CONTENTS
Nese Hayat AKSOY, PhD Aksaray University, School of Health and Hacettepe
University, Faculty of Medicine, Department of Biochemistry. nhaksoy@
aksaray.edu.tr ABSTRACT Aldolase catalyses the reaction of cleavage of
fructose 1,6-bisphosphate (F-1,6-BP) into glyceraldehyde 3-phosphate and
dihydroxyacetone phosphate (DHAP), that is part of glycolysis. Class I (Schiff
base) type aldolase (EC 4.1.2.13) is generally found in mammals, protozoa and
higher plants while Class II type, metalloenzyme, is present in bacteria, fungi
and blue green algae. The mammalian aldolases have the key catalytic amino
acid residues involved in the reaction are lysine and tyrosine. Many bacteria use
two magnesium or zinc ions in place of the lysine. Also zinc ion increased the
intracellular concentration of fructose-1-P in hepatocytes incubated with fructose,
indicating a more potent zinc inhibition of aldolase. In this study, we carried out
inhibition effects of bivalent ion on Fructose-1,6-bisphosphate aldolase. We have
investigated the interaction of human placental aldolase with bivalent Zn+2 metal.
It was defined that, Zn+2 is competitive inhibitor of healthy human placental
FBPA. Ki values of healthy human placental aldolase for Zn+2 ion was confirmed
11.377±1.372 mM
Nese Hayat AKSOY, PhD Aksaray University, School of Health and Hacettepe
University, Faculty of Medicine, Department of Biochemistry. nhaksoy@aksaray.
edu.tr Aldolase catalyses the reaction of cleavage of fructose 1,6-bisphosphate
(F-1,6-BP) into glyceraldehyde 3-phosphate and dihydroxyacetone phosphate
(DHAP), that is part of glycolysis. Class I (Schiff base) type aldolase (EC
4.1.2.13) is generally found in mammals, protozoa and higher plants while Class
II type, metalloenzyme, is present in bacteria, fungi and blue green algae. The
mammalian aldolases have the key catalytic amino acid residues involved in the
reaction are lysine and tyrosine. Many bacteria use two magnesium or zinc ions
in place of the lysine. Also zinc ion increased the intracellular concentration of
fructose-1-P in hepatocytes incubated with fructose, indicating a more potent zinc
inhibition of aldolase. In this study, we carried out inhibition effects of bivalent
ion on Fructose-1,6-bisphosphate aldolase. We have investigated the interaction
of human placental aldolase with bivalent Zn+2 metal. It was defined that,
Zn+2 is competitive inhibitor of healthy human placental FBPA. Ki values of
healthy human placental aldolase for Zn+2 ion was confirmed 11.377±1.372 mM
Turk J Biochem, 2012; 37 (S1)
http://www.TurkJBiochem.com