Activation of thiamine diphosphate in pyruvate decarboxylase from Zymomonas mobilis.

doi:10.1016/s0014-5793(98)01594-4

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Article

Activation of thiamine diphosphate in pyruvate decarboxylase from Zymomonas mobilis.

FEBS letters - 28 Dec 1998

Tittmann K, Mesch K, Pohl M, Hübner G

Abstract excerpt

Replacement of tryptophan 392 located in the active site cavity of pyruvate decarboxylase (PDC; EC 4.1.1.1) from Zymomonas mobilis by methionine or glutamine yields enzymes with smaller catalytic constants of 8.5 s(-1) and 3.6 s(-1) at 4 degrees C, compared to that of the wild-type enzyme (17 s(-...

Topics

Hydrogen-Ion Concentration
Kinetics
Mutation
Protons
Pyruvate Decarboxylase
Thiamine Pyrophosphate
Zymomonas

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