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. Author manuscript; available in PMC: 2009 Aug 12.
Published in final edited form as: Biochemistry. 2008 Jul 16;47(32):8271–8282. doi: 10.1021/bi800212b

Table 2.

Kinetic Parameters of the Glycine Hinge Mutations

Enzyme Km (µM) kcat(sec−1) Ki(µM) kcat/Km(M−1 sec−1) Serine I 0.5b (µM) Hill Coefficient
Native 170 ± 50 2461 ± 281 950 ± 120 1.4 × 107 36 ± 6 1.8 ± 0.1
G316V 114 ± 4 1111 ± 30 2231 ± 190 1.0 × 107 23 ± 4 1.6 ± 0.1
G317V 165 ± 9 2111 ± 119 1110 ± 148 1.3 × 107 23 ± 3 1.5 ± 0.1
G318V 203 ± 23 2349 ± 177 1925 ± 437 1.2 × 107 166 ± 22 2.5 ± 0.1
G316, 317V 610 ± 95 2805 ± 310 380 ± 45 0.5 × 107 75 ± 17 1.7 ± 0.1
G317, 318V 220 ± 43 605 ± 27 1620 ± 402 0.3 × 107 53 ± 12 1.9 ± 0.1
G316, 318V 470 ± 43 2827 ± 197 220 ± 35 0.6 × 107 18 ± 5 1.9 ± 0.1
G316,317, 318Va
a

No detectable protein produced

b

All mutants are able to be inhibited by serine to < 95%.