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. 2005 Jun;71(6):3276–3284. doi: 10.1128/AEM.71.6.3276-3284.2005

TABLE 5.

Substrate specificity of the ARO10-dependent 2-oxo-acid-decarboxylase activity in S. cerevisiaea

Substrate Enzyme activity nmol min−1 (mg protein)−1
IMZ0001 [(NH4)2SO4c] IMZ002 [(NH4)2SO4c] IMZ002 [phenylalaninec] Ratiob
Phenylpyruvate BDd 61.75 ± 1.71 (100) 270 ± 6.98 (100) 4.37
α-Ketoisovalerate BD 16.75 ± 2.21 (27) 78.25 ± 4.1 (29) 4.67
α-Ketoisocaproate BD 25 ± 0.82 (40) 118 ± 7.53 (44) 4.72
α-Ketomethylvalerate BD 21 ± 1.63 (34) 97 ± 6.68 (36) 4.62
3-Methylthio-α-ketobutyrate BD 18.5 ± 1.29 (30) 87.7 ± 7.69 (32) 4.74
Pyruvate BD BD BD
a

Strain IMZ001 is pdc1Δ pdc5Δ pdc6Δ aro10Δ thi3Δ carrying the empty expression vector p426GPD (2μ URA3 TDH3p). Strain IMZ002 is the same strain carrying the plasmid pUDe001 (2μ URA3 TDH3p-ARO10). Both strains were grown in aerobic, ethanol-limited chemostat cultures with ammonia as the nitrogen source. Enzyme activities were assayed in cell extracts. Data are the average±average deviation of the mean from assays of two independent chemostat cultures. The relative 2-oxo acid activities, expressed as a percentage of phenylpyruvate activity, are in parentheses.

b

Ratio of phenylalanine versus (NH4)2SO4.

c

N source.

d

BD, below detection limit.

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