Figure 2

Comparison of the fractions of corresponding intact bonds in amino acid precursors Oaa, Oga and Pep in T. reesei. The data is taken from all replicates of fractional [U-¹³C]glucose or [U-¹³C]sorbitol experiments performed (1-3 wild type on glucose, 4-6 Δcre1 on glucose, 7-9 wild type on sorbitol, 10-12 wild type on sorbitol (sophorose experiment control), 13-15 wild type on sorbitol (sophorose induction), 16-17 Δcre1 on sorbitol (sophorose experiment control), 18-19 Δcre1 on sorbitol (sophorose induction)). Oaa data was detected from Asp-Cα, -Cβ and Thr-Cα, Oga data from Glu-Cα, -Cβ and Pro-Cα, -Cβ and Pep data from Phe and Tyr-Cα. Fractions of intact bonds in Oaa, Oga and Pep were calculated from combinations of fragmentomers. A) OAA_x1x is the fraction of Oaa molecules with an intact bond at C2-C3, OGA_x1xx is the fraction of Oga molecules with an intact bond at C2-C3 and PEP_x1 is the fraction of Pep molecules with an intact bond at C2-C3. B) OAA_xx1 is the fraction of Oaa molecules with an intact bond at C3-C4 and OGA_1xxx is the fraction of Oga molecules with an intact bond at C1-C2. Error bars are ± SEMs. The carbon chain of Oaa_mit remains intact in the TCA cycle except that C1 is cleaved in the synthesis of Oga. Almost the entire labeling pattern of Oaa_mit can be assessed from the labeling pattern determined for Oga. If Asp and Thr synthesis originates from Oaa_mit, the fractions of corresponding Oaa and Oga intact fragments in the figures should match.