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. 2011 May 25;286(29):26061–26070. doi: 10.1074/jbc.M111.227595

TABLE 2.

Kinetic parameters of WT and mutant carrot HPPD

For clarity, mutated residues are numbered according to the Arabidopsis crystal structure 1SQD (21). The conserved residues Ser-260, Asn-275, Gln-286, Gln-300, and Gln-372 of the carrot HPPD mutated in this study correspond thus to Ser-246, Asn-261, Gln-272, Gln-286, and Gln-358 of the Arabidopsis HPPD (1SQD), respectively (see Table 1).

Enzyme kcat KM-HPP
s1 μm
WT 1.8 7.5 ± 2.5
Q358E 2.1 286 ± 22
Q286E 0.1 551 ± 76
Q272E 0.2 452 ± 63
N261D 0.3 153 ± 32
S246A 0.2 9 ± 3