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. 2004 Feb;16(2):353–366. doi: 10.1105/tpc.019372

Table 3.

Kinetic Parameters of Recombinant AGD2- and ALD1-Catalyzed Reactions for Amino Acid Degradation Using Either Lys, Ala, or Arg with2-Oxoglutarate

Substrate Cosubstrate (mM) Km (mM) kcat (s−1) kcat/Km (mM−1 s−1)
AGD2 Lys 2-oxoglutarate (100 mM) 58.8 5.33 0.091
AGD2P398S Lys 2-oxoglutarate (100 mM) 71.4 2.87 0.040
ALD1 Lys 2-oxoglutarate (50 mM) 0.53 4.42 8.34
AGD2 2-oxoglutarate Lys (100 mM) 1.82 2.83 1.55
AGD2P398S 2-oxoglutarate Lys (100 mM) 1.92 1.83 0.95
ALD1 2-oxoglutarate Lys (100 mM) 2.63 3.75 1.43
AGD2 Ala 2-oxoglutarate (100 mM) 25.6 1.67 0.065
AGD2P398S Ala 2-oxoglutarate (100 mM) 23.3 0.87 0.037
ALD1 Ala 2-oxoglutarate (100 mM) 5.56 2.15 0.39
AGD2 Arg 2-oxoglutarate (100 mM) 154 0.69 0.0045
AGD2P398S Arg 2-oxoglutarate (100 mM) 167 0.35 0.0021
ALD1 Arg 2-oxoglutarate (100 mM) 5.10 2.07 0.41

Km values were obtained from the initial velocity data and Lineweaver-Burk plots. kcat was calculated using equation Vmax = kcat [Enzyme]. Three independent measurements were averaged.