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. 2008 Sep 26;283(39):26591–26601. doi: 10.1074/jbc.M801703200

TABLE 3.

Kinase activity of p38α in different phosphorylation states with ATF2Δ109 as a substrate (pH 7.0, 1 mm ATP, 10 mm Mg2+, 25°C)

kcat Km kcat/Km
s–1 μm m–1 s–1
p38α/pTpY 4.7 ± 0.3 2.03 ± 0.34 (2.3 ± 0.5) × 106
p38α/pT 3.8 ± 0.3 20.1 ± 3.2 (1.9 ± 0.5) × 105
p38α/pY 2497 ± 382
p38α 691 ± 34