1                                  The >40,000-fold diminution in kcat for the Asp-204 mutants and the

2 e diphosphate, is characterized by a >42,000-fold diminution in k(cat), indicating the critical invol

3 heoretical explanation for the observed 1000-fold diminution in the rate of 5-55 disulfide bond forma

4                         The approximately 13-fold diminution in activity because of the mutation corr

5                              For R173Q, a 15-fold diminution in Vmax and a 100-fold increase in Km Ru

6  phenylalanine or alanine results in a 10(3)-fold diminution of k(cat) and suppression of the overall

7 ion, electronically excited DA manifests a 3-fold diminution of S(1)-->S(0) oscillator strength on a

8 with dThd as substrate, apart from Y21E (350-fold diminution in the k(cat)/K(m)).

9 f the wild-type enzyme, their observed 10(4)-fold diminution in catalytic efficiency supports assignm

10   Kinetic characterization indicated > 10(4)-fold diminution in V/KRu5P for R168Q, attributable to a

11 ein, whereas E193Q is stable, exhibiting >50-fold diminution in Vm and elevated Km values for ATP (ap

12                              The observed 56-fold diminution in affinity for the mutant enzyme suppor

13 serines 36, 120, 153, and 155 are modest (<8-fold diminution in k(cat)).