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. Author manuscript; available in PMC: 2010 May 11.
Published in final edited form as: Cell Mol Life Sci. 2009 Oct 15;67(3):353–368. doi: 10.1007/s00018-009-0166-4

Table 3.

Major biochemical differences of four KATs

Optimal pH range Recommended assay pH Recommended co-substrate Specific inhibitors of KAT activity Unique substrates
KAT I 7.5–10 9–10 Glyoxylate Tryptophan
3-indolepropionic acid
dl-indole-3-lactic acid
KAT II 7–9 7–8 α-ketoglutarate (S)-4-ethylsulfonylbenzoylalanine (rat KAT II) Aminoadipate
KAT III 9–10 (mouse) 9–10 (mouse) Glyoxylate Methionine (mouse)
KAT IV 7–9 (mouse) 7–8 (mouse) α-ketoglutarate Aspartate (mouse) Aspartate (mouse)

Unless specified, the listed parameters are for human enzymes