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Table 1 Kinetic parameters of Mt MetAPs

From: Amino-terminal extension present in the methionine aminopeptidase type 1c of Mycobacterium tuberculosis is indispensible for its activity

System

Km(mM)

kcat(s-1)

kcat/Km(mM-1s-1)

No. of experiments

Mt MetAP1a (MGMM)

2.85 ± 0.69

9.63 ± 1.42

3.47 ± 0.7

3

Mt MetAP1a (MAS)

3.3 ± 0.35

11.17 ± 0.97

3.32 ± 0.18

4

Mt MetAP1c (MAS)

1.36 ± 0.25

1516 ± 174

1156 ± 317

4

  1. Enzyme assays were carried out as described under 'Methods' following the incubation of purified Mt MetAP1a (1.7 nM/reaction) or Mt MetAP1c (0.038 nM/reaction) proteins with different concentrations (0.75-8 mM) of Met-Ala-Ser (MAS) or Met-Gly-Met-Met (MGMM) as substrate. Km and Vmax values were calculated from Non-linear regression analysis by fitting the data to Michaelis-Menten equation, and the results are expressed as mean ± SD. For calculating kcat values, the molecular mass of recombinant enzyme(s) was considered as 29.5 kDa (for Mt MetAP1a) or 33.1 kDa (for Mt MetAP1c). Mean ± SD for kcat/Km was determined after calculating it for individual experiment.