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. Author manuscript; available in PMC: 2007 Aug 13.
Published in final edited form as: Proteins. 2005 Jan 1;58(1):14–21. doi: 10.1002/prot.20293

TABLE II.

Effect of Mutations on the Stability of Tyrosine Hydroxylase

Enzyme Apparent
Tme
ΔTmf kinacta (min−1)
Wild-type 48.2 ± 0.3 0 0.0068 ± 0.0014
 (53.9 ± 1.0)b
T245P 44.3 ± 0.1 3.9 ± 0.3 0.020 ± 0.001
T283M ndc nd 0.330 ± 0.026
R306H  45.8 ± 0.1b  8.2 ± 1.1d 0.142 ± 0.007
T463M 40.6 ± 0.1 7.7 ± 0.3 0.090 ± 0.003
a

First order rate constant for loss of activity at 50°C.

b

Buffer contained 10% glycerol.

c

nd, not determined.

d

Compared to wild-type enzyme in the presence of 10% glycerol.

e

Determined from a fit of the data to Equation (3).

f

Difference in apparent Tm from wild-type enzyme.