Skip to main content
. Author manuscript; available in PMC: 2010 Jun 9.
Published in final edited form as: Biochemistry. 2009 Jun 9;48(22):4959–4971. doi: 10.1021/bi900432n

Table 4.

Kinetic Parameters of CPS Double-Site Mutantsa

CPS mutant kcat (s−1) −Δ Km
(mM)		 +Δ kcat/Km
(mM−1 s−1)		 −Δ
Y345F/E380D 0.0059 ± 0.0001 61 0.49 ± 0.06 1.4 0.012 ± 0.001 86
Y345F/E380Q 0.011 ± 0.001 33 0.9 ± 0.2 2.6 0.011 ± 0.001 95
Y345A/E380A 0.0051 ± 0.0004 71 0.40 ± 0.01 1.1 0.012 ± 0.001 87
a

Steady-state rate constants determined using the PPi coupled enzyme assay at pH 8.0. +Δ refers to the fold change above the Km,CMPr listed for wild-type CPS and −Δ to the fold change below the kcat or kcat/Km,CMPr of wild-type CPS.