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. 2012 Oct 31;287(52):43262–43269. doi: 10.1074/jbc.M112.416453

TABLE 1.

MIC data, steady-state kinetic parameters, and dissociation constants for AAC(6′)-Ie/APH(2″)-Ia

Aminoglycoside MICa kcat Km kcat/Km Kib
μg/ml s1 μm m1 s1 μm
4,6-Disubstituted
    Kanamycin A 512/4 0.57 ± 0.02 <1 >5.7 × 105
    Kanamycin B 64/1 0.12 ± 0.01 <1 >1.2 × 105
    Tobramycin 64/0.5 0.11 ± 0.01 <1 >1.1 × 105
    Dibekacin 32/0.5 0.15 ± 0.01 0.3 ± 0.2 (5 ± 4) × 105
    Arbekacin 0.5/0.25 2.3 ± 0.1 0.8 ± 0.2 (2.9 ± 0.7) × 106
    Amikacin 4/2 3.7 ± 0.1 33 ± 4 (1.1 ± 0.1) × 105
    Gentamicin C 32/0.25 3.0 ± 0.1 0.6 ± 0.3 (5 ± 2) × 106
    Sisomicin 16/0.25 8.1 ± 0.2 0.8 ± 0.2 (1.0 ± 0.2) × 107
    Netilmicin 2/0.25 6.5 ± 0.1 0.41 ± 0.05 (1.6 ± 0.2) × 107

4,5-Disubstituted
    Neomycin B 1/0.5 0.26 ± 0.02
    Paromomycin 4/4 5.3 ± 0.3
    Lividomycin A 8/4 11 ± 1
    Butirosin A and B 140 ± 10

Atypical
    Neamine 16/8 0.10 ± 0.01

a Ratio of the MICs with E. coli JM83 harboring pBluescript::AAC(6′)-Ie/APH(2″)-Ia to the E. coli JM83 host strain.

b Dissociation constant for the binary enzyme·GTP complex.