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Table 1 Ki values and type of inhibition for the interaction of a dead-end inhibitor (FTA) and reaction products (AdoHCy, AFCME) with Icmt. The Km values obtained for the two substrates of the reaction, BFC and AdoMet, are also shown for comparaison.

From: Analysis of the kinetic mechanism of recombinant human isoprenylcysteine carboxylmethyltransferase (Icmt)

Substrate\Inhibitor

AdoHcy

FTA

AFCME

BFC

Competitive

Competitive

Noncompetitive

Km = 2.1 ± 0.4 μM

3.59 ± 1.03 μM

1.17 ± 0.16 μM

1.91 ± 0.65 μM

AdoMet

Competitive

Uncompetitive

Mixed-type

Km = 7.8 ± 1.2 μM

3.54 ± 1.12 μM

 

2.43 ± 0.70 μM