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

TABLE 6.

Regulation of decarboxylase activities in the reference S. cerevisiae strain IME004 (CEN.PK113-5D, p426GPD) and in an isogenic strain expressing a multicopy plasmid-borne ARO10 gene from a constitutive TDH3 promoter, strain IME003a

Substrate for decarboxylase assay IME004 [ura3 p426GPD (URA3)]
IME003 [ura3 pUDe001 (URA3 TDH3p-ARO10)]
Ethanol
Glucose
Ethanol
Glucose
(NH4)2SO4 Phenylalanine (NH4)2SO4 Phenylalanine (NH4)2SO4 Phenylalanine (NH4)2SO4 Phenylalanine
Phenylpyruvate BDb 64 ± 1.2 BD 67.5 ± 0.7 35 ± 5.7 76.5 ± 1.5 BD 82.75 ± 26.73
α-Ketoisovalerate BD 17 ± 2.2 BD 19 ± 0 19 ± 0 21.75 ± 1.7 BD 22.4 ± 6.4
α-Ketoisocaproate BD 28 ± 3.1 BD 29.5 ± 0.7 15 ± 1.4 30.5 ± 3 BD 31.5 ± 9.8
α-Ketomethylvalerate BD 23 ± 0.7 BD 25.7 ± 3.8 12.5 ± 0.7 28 ± 4.0 BD 28.3 ± 13.6
3-Methylthio-α-ketobutyrate BD 20.5 ± 1.2 BD 22 ± 0 11 ± 0 23.5 ± 1.2 BD 24.25 ± 9.1
a

Both strains were grown in aerobic, carbon-limited chemostat cultures with glucose or ethanol as a carbon source and ammonia or phenylalanine as a carbon source and ammonia or phenylalanine as a nitrogen source. Enzyme activities were assayed in cell extracts of independent duplicate cultures and are expressed as nmol·min−1·(mg protein)−1. Data are presented as average ± average deviation of the mean of two chemostat cultures.

b

BD, below detection limit.