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. Author manuscript; available in PMC: 2012 Aug 1.
Published in final edited form as: Proteins. 2011 Jun 2;79(8):2455–2466. doi: 10.1002/prot.23069

Table 4.

Effects of mutations on the kinetic parameters of GDPMK with Mg2+ activation and GDP-mannose as substrate at pH 8.5 and 37° C

kcat (s−1) Km (μM)
WT 90.2±6.7 659±65
E151A 21.3±4.6 594±140
K176A 0.11±0.04 >1200
R44S 1.69±0.12 >1200
E100A <0.01 NDa
E149A 80.6±6.3 555±85
D150A 126.4±14.2 NDa
D152A 42.6±6.1 NDa
Q65A 24.4±17.4 NDa
a

: The Kms labeled “ND” were not determined. In the case of E100A the activity was too low to be measured