Abstract
The circular dichroism of transketolase from baker's yeast was examined in the 400 to 200 nm region in the presence and absence of its coenzyme and substrates. Coenzyme binding caused an extrinsic Cotton effect v pyrophosphate and a tryptophan moiety of the enzyme protein. Addition of donor substrates as D-fructose-6-phosphate and hydroxy-pyruvate abolished the ellipticity band at 235 nm. Steric hindrance might be responsible for the fact that 2-(1,2-dihydroxyethyl) thiamine pyrophosphate (“active glycolaldehyde”) can no longer form a charge transfer complex. On the other hand, acceptor substrates in the transketolase reaction, such as ribose-5-phosphate, did not influence the broad negative dichroism at 325 nm.
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