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Table 3 Biochemical properties of the XcNAGS-K with respect to its synthase activity.

From: A novel bifunctional N-acetylglutamate synthase-kinase from Xanthomonas campestris that is closely related to mammalian N-acetylglutamate synthase

  

XcNAGS-Ka

H6XcNAGS-Kb

AcCoA

Vmax e (μmoles min-1 mg-1)

58.1 ± 6.2 c

61.6 ± 7.6

 

Kmapp (mM)

1.3 ± 0.4

1.5 ± 0.5

 

h

1.9 ± 0.4

2.0 ± 0.5

Glu

Vmax e (μmoles min-1 mg-1)

45.4 ± 1.8 d

52.8 ± 1.2

 

Kmapp (mM)

2.8 ± 0.5

3.5 ± 0.4

  1. aXcNAGS-K without affinity tag bXcNAGS-K with the polyhistidine tag and thrombin protease recognition sequence cvalues for AcCoA represent fitting parameters to Hill equation and the associated errors dvalues for glutamate represent fitting parameters to Michaelis-Menten equation and the associated errors ethe Vmax-values apply to infinite concentrations of glutamate and AcCoA only, not all substrates
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BMC Biochemistry

ISSN: 1471-2091

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