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Title: Studies on biotin dependent carboxylases and the properties of carboxybiotin

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:5220373

Biotin dependent carboxyl-transfer reactions have been studied using biotin and pyruvate carboxylases. The pH profile for the Mg/sup 2 +/ and MgATP dependent carboxylation of biotin by bicarbonate shows that an enzymic base with a pK of 6.5 must be unprotonated for catalysis to occur. The pH profiles for the carboxyl-transfer reaction of pyruvate carboxylase have been obtained by studying the decarboxylation of oxalacetate stimulated by the presence of oxamate. Similarly, /sup 13/C and /sup 2/H isotope effects have been measured for the decarboxylation of oxalacetate by both enzymic and nonenzymic means. From these studies the authors can conclude that carboxyl-transfer between biotin and oxalacetate is at least partially rate-limiting and is not concerted with proton-transfer. The lack of any apparent enzymic acid-base catalyst (the V/K profile for oxalacetate is pH independent) suggests that proton transfer may occur directly between biotin and the carbanion formed when oxalacetate is decarboxylated. The pH profile for the nonenzymatic decarboxylation of carboxybiotin shows a plateau below pH 4 (k = 0.012 min/sup -1/ at 2/sup 0/C), and a lower plateau above pH 8 (k = 0.005 min/sup -1/ at 25/sup 0/C). A proton inventory at low pH is linear, while at high pH it is curved. These data suggest that two different mechanisms operate at high and low pH.

Research Organization:
Univ. of Wisconsin, Madison
OSTI ID:
5220373
Report Number(s):
CONF-8606151-
Journal Information:
Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Vol. 45:6; Conference: 76. annual meeting of the Federation of American Society for Experimental Biology, Washington, DC, USA, 8 Jun 1986
Country of Publication:
United States
Language:
English