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. 2005 Mar;187(6):2077–2083. doi: 10.1128/JB.187.6.2077-2083.2005

TABLE 3.

Substrate specificity of native and recombinant P. furiosus lysine aminopeptidase

Substratea (with p-nitroanilide amino acids) % Relative activityb for:
n-KAP r-KAP
Lys-pNA 100 100
Arg-pNA 34 47
Leu-pNA 0 7
Pro-pNA 0 6
Ala-pNA 0 3
Gly-pNA 4 0.7
His-pNA 5 0
Phe-pNA 14 0
Ac-Phe-pNA 4 0
a

All substrates were used at a final concentration of 10 mM.

b

The rate of hydrolysis is expressed as a percentage of the activity compared to that obtained by using Lys-pNA as the substrate at 100°C, where 100% activity corresponds to 1,900 and 2,200 U/mg for native and recombinant KAP, respectively.