ENZYMOLOGICAL PROPERTIES OF PANTOTHENATE SYNTHETASE FROM ESCHERICHI A COLI B

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概要

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• Following a previous report on physicochemical properties, the enzymological properties of a homogeneously purified preparation of pantothenate synthetase were described. The optimum pH was 10.0 and optimum temperature 30°C. The lyophilized enzyme was very stable on standing at -20°C. K+ or NH4+ and Mg2+ or Mn2+ were required as activators; other cations examined were inhibitive to various extents and the enzyme required ATP as the energy supplier. Some co-amino acids exerted strong inhibition, and the enzyme was inhibited by some chelating agents but was not affected by SH compounds and SH inhibitors. Apparent Km for pantoate was 6.3×10-5M, for β-alanine 1.5×10-4 M, and for ATP 1.0×10-4M, According to the method of CLELAND, the enzyme reaction proceeds by a Bi Uni Uni Bi Ping Pong mechanism and a scheme showing the order of binding of substrates and releasing of products is presented.

• 財団法人 学会誌刊行センターの論文

著者

• 宮武 和孝

  Department of Applied Biological Chemistry, Graduate School of Agriculture and Biological Sciences,

• 中野 長久

  Department of Applied Biological Chemistry, College of Agriculture, University

• 北岡 正三郎

  Department of Agricultural Chemistry, University of Osaka Prefecture

• 宮武 和孝

  Department of Agricultural Chemistry, University of Osaka Prefecture

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