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. 2009 Oct 12;54(1):267–272. doi: 10.1128/AAC.00553-09

TABLE 3.

Kinetic parameters of P. aeruginosa and M. barkeri PBGSs and IC50s for alaremycina

Parameter P. aeruginosa M. barkeri
General catalytic properties
    Km(μM) 0.32 0.07
    kcat (s−1) 16.1 0.012
    kcat/Km (μM−1s−1) 50.3 0.17
Inhibition by alaremycin
    IC50 (mM) 2.1 2.2
    ki (mM) 1.33 1.51
a

The Michaelis-Menten constant (Km) and the kcat and the kcat/Km values for the PBGSs were determined from substrate velocity plots by measuring the constant velocity formation of porphobilinogen from ALA over a substrate concentration range of from 1 to 10 mM. Values were determined by the use of iterative, curve-fitting Lineweaver-Burk plots (SigmaPlot program, version 8.0; Enzyme Kinetics program, version 1.1). For inhibition studies, 0 to 40 mM alaremycin was added to the enzyme activity test. The standard errors of the results were between 5 and 10%.