Please use this identifier to cite or link to this item: https://doi.org/10.1021/pr060575g
Title: Proteome analysis of Sulfolobus solfataricus P2 propanol metabolism
Authors: Poh, K.C. 
Burja, A.M.
Radianingtyas, H.
Fazeli, A.
Wright, P.C.
Keywords: Alcohol dehydrogenase
Alcohol metabolism
iTRAQ
Shotgun proteomics
Stable isotope labeling
Sulfolobus solfataricus P2
Issue Date: Apr-2007
Citation: Poh, K.C., Burja, A.M., Radianingtyas, H., Fazeli, A., Wright, P.C. (2007-04). Proteome analysis of Sulfolobus solfataricus P2 propanol metabolism. Journal of Proteome Research 6 (4) : 1430-1439. ScholarBank@NUS Repository. https://doi.org/10.1021/pr060575g
Abstract: Sulfolobus solfataricus P2 is able to metabolize n-propanol as the sole carbon source. An average n-propanol consumption rate of 9.7 and 3.3 mg/L/hr was detected using GC-MS analysis from S. solfataricus cultures grown in 0.40 and 0.16% w/v n-propanol, respectively. The detection of propionaldehyde, the key intermediate of n-propanol degradation, produced at a rate of 1.3 and 1.0 mg/L/hr in 0.40 and 0.16% w/v n-propanol cultures, further validated the ability of S. solfataricus to utilize n-propanol. The translational and transcriptional responses of S. solfataricus grown on n-propanol versus glucose were also investigated using quantitative RT-PCR and iTRAQ approaches. Approximately 257 proteins with ≥2 MS/MS spectra were identified and quantified via iTRAQ. The global quantitative proteome overview obtained showed significant up-regulation of acetyl-CoA synthetases, propionyl-CoA carboxylase, and methylmalonyl-CoA mutase enzymes. This led to the proposition that the propionyl-CoA formed from n-propanol degradation is catabolised into the citrate cycle (central metabolism) via succinyl-CoA intermediates. In contrast, evidence obtained from these analysis approaches and in vivo stable isotope labeling experiments, suggests that S. solfataricus is only capable of converting isopropyl alcohol to acetone (and vice versa) but lacks the ability to further metabolize these compounds. © 2007 American Chemical Society.
Source Title: Journal of Proteome Research
URI: http://scholarbank.nus.edu.sg/handle/10635/109556
ISSN: 15353893
DOI: 10.1021/pr060575g
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