Table 3 Apparent Michaelis-Menten constants for phLDH and rmLDH with rmGAPDH-NADH or byGAPDH-NADH complex as substrate:.

From: Substrate Channeling via a Transient Protein-Protein Complex: The case of D-Glyceraldehyde-3-Phosphate Dehydrogenase and L-Lactate Dehydrogenase

 

phLDH

rmLDH

Measurement type:

rmGAPDH-NADH

rmGAPDH-NADH

Vmax, units per milligrama

6.5 ± 0.4

8.2 ± 0.7

KM, μMb

59.6 ± 6

35 ± 7

Measurement type:

byGAPDH-NADH

byGAPDH-NADH

Vmax, units per milligrama

192 ± 10

241 ± 3

KM, μMb

116 ± 8

78 ± 2

  1. aone units is equivalent of 1 micromole NADH oxidized per minute; bMeasured Michaelis-Menten parameters depend on pyruvate concentrations, we measured phLDH and rmLDH activity in the presence of 630 μM pyruvate.
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