Figure 3.
Fig. 3. Phosphotransfer efficiency of NDPK-A and mutants
for nucleoside analogs. The rates of phosphorylation of pure
recombinant NDP kinases (1 µM) were measured at the
pre-steady state in a fluorescence stopped-flow with d4TTP. The
catalytic efficiency (expressed in M 1s 1) was
determined from the variation of the rate as a function of
analog as shown in Fig. 2: NDPK-A ( ), N115S (
), L55H
( ),
Dictyostelium ( ), and
L55H-N115S ( ). B,
catalytic efficiencies of NDPK-A ( ) and the
mutants L55H ( ), N115S
( ), and
L55H-N115S ( ) for
several antiviral analog triphosphate derivatives. The values
were extracted from stopped-flow experiments as shown in A for
d4TTP.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2002,
277,
39953-39959)
copyright 2002.
1s 
), N115S (
), L55H
( 
),
Dictyostelium ( 
), and
L55H-N115S ( 
). B,
catalytic efficiencies of NDPK-A ( 
) and the
mutants L55H ( 
), N115S
( 
), and
L55H-N115S (