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. Author manuscript; available in PMC: 2011 Aug 1.
Published in final edited form as: Biochemistry. 2010 Aug 3;49(30):6485–6493. doi: 10.1021/bi100648w

Table 2.

Kinetic Parameters for Alternate Substratesa

AC5C AC6C


kmax
(s−1)
Kapp
(mM)
kmax
(s−1)
Kapp
(mM)


R406M 9.4 (0.9) × 10−4 15 (6) 5 (1) × 10−4 140 (50)
WTb 0.98 (0.03)c 4.0 (0.8) 2.3 (0.2)c 53 (150)
a

Errors are given in parentheses.

b

WT values taken from (Sun 37, 3865).

c

The values given for WT are steady-state kcat and Km values; it is assumed that the decarboxylation half-reaction is rate limiting in WT for AC5C and AC6C, so that kcat = kmax.