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. Author manuscript; available in PMC: 2014 Oct 22.
Published in final edited form as: Biochemistry. 2013 Oct 8;52(42):10.1021/bi401117y. doi: 10.1021/bi401117y

Table 2.

Kinetic Parameters from Scheme 4 for the Decarboxylation Reactions of the Substrate Pieces Catalyzed by Wildtype and R235A Mutant ScOMPDC.a

ScOMPDC EO + HPO32− FEO + HPO32−

(kcat/Km)E
(M−1 s−1)
(kcat/Km)EHPiKd
(M−2 s−1)
(kcat/Km)E
(M−1 s−1)
(kcat/Km)EHPiKd
(M−2 s−1)
Wildtype b 0.026 1.2 × 104 10 4.8 × 104
R235A 0.026 c 0.63 c 12 250 ± 15
a

The second-order rate constants reported in this Table are reproducible to better than ± 10%.

b

The data for the wildtype ScOMPDC catalyzed reactions of EO and FEO are from Ref. 19 and 28, respectively.

c

Ref. 19.