Table 2 Kinetic parameters of wild type and six MtbGmhA mutants obtained using Michaelis Menten curve and Lineweaver–Burk plot (in red bracket). The kinetic parameters of E. coli. GmhA, B. pseudomallei GmhA and H. pyroli GmhA are shown for comparative analysis.

From: Structural and functional characterization of M. tuberculosis sedoheptulose- 7-phosphate isomerase, a critical enzyme involved in lipopolysaccharide biosynthetic pathway

Protein

Km (mM)

kcat (s−1)

kcat/Km (mM−1 s−1)

MtbGmhA

0.31 ± 0.06 (0.38)

0.45 ± 0.02 (0.52)

1.45 (1.36)

N53G mutant

0.67 ± 0.15 (0.62)

0.27 ± 0.02 (0.27)

0.40 (0.43)

S121G mutant

0.76 ± 0.17 (0.73)

0.36 ± 0.03 (0.33)

0.47 (0.45)

S123A mutant

0.92 ± 0.23 (0.93)

0.31 ± 0.03 (0.33)

0.33 (0.35)

S126A mutant

0.83 ± 0.22 (0.83)

0.19 ± 0.02 (0.18)

0.22 (0.21)

T122A mutant

0.90 ± 0.4 (0.89)

0.09 ± 0.02 (0.11)

0.10 (0.12)

Q173A mutant

1.53 ± 0.6 (1.54)

0.10 ± 0.02 (0.13)

0.06 (0.08)

E. coli GmhA

0.9 ± 0.3

0.4 ± 0.7

0.5

B. pseudomallei GmhA

0.4 ± 0.2

0.5 ± 0.1

1.2

H. pylori GmhA

0.5 ± 0.1

33.1 ± 2.1

71.9

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