Table 4 Inhibitor Data for AgmNATa ,b.

From: Structural and Mechanistic Analysis of Drosophila melanogaster Agmatine N-Acetyltransferase, an Enzyme that Catalyzes the Formation of N-Acetylagmatine

Inhibitor

Varied Substrate

Constant Substrate

Inhibitor Patternc

Ki,s

Ki,i

Arginine methyl

Acetyl-CoA

Agmatine (0.3 mM)

UC

1.5 ± 0.1 mM

2.9 ± 0.1 mM

ester

Agmatine

Acetyl-CoA (0.1 mM)

C

Arcaine

Acetyl-CoA

Agmatine (0.3 mM)

UN

28 ± 1 μM

34 ± 1 μM

Agmatine

Acetyl-CoA (0.1 mM)

C

N-Acetylagmatine

Acetyl-CoA

Agmatine (0.3 mM)

UC

160 ± 30 μM

420 ± 20 μM

Agmatine

Acetyl-CoA (0.1 mM)

C

Oleoyl-CoA

Acetyl-CoA

Agmatine (0.3 mM)

C

19 ± 1 μM

67 ± 4 μM

Agmatine

Acetyl-CoA (0.1 mM)

NC

67 ± 4 μM

  1. aDetails for each set of inhibition experiments are provided in the legends to appropriate figures included in the supplementary figures. bInhibition constants are reported as ± standard error. cC = Competitive inhibition, NC = noncompetitive inhibition, and UC = uncompetitive inhibition
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