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User:Scott Mazurkewich

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Post Doctoral Researcher at the Department of Biology and Biological Engineering, Chalmers University of Technology.

Background

Scott obtained both his BSc and PhD from the University of Guelph in Canada. His PhD work, completed under the supervision of Stephen Seah, was on structure-function studies of enzymes involved in the metabolism of aromatic lignin fragments in Pseudomonas [1, 2, 3]. Shortly after completing his PhD studies, he started a post-doctoral research position with Johan Larsbrink at Chalmers University. There he has been working collaboratively with Jenny Arnling Bååth and Leila Lo Leggio on structure-function studies of bacterial CE15 members.

Selected papers

  1. Wang W, Mazurkewich S, Kimber MS, and Seah SY. (2010) Structural and kinetic characterization of 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate aldolase, a protocatechuate degradation enzyme evolutionarily convergent with the HpaI and DmpG pyruvate aldolases. J Biol Chem. 285, 36608-15. DOI:10.1074/jbc.M110.159509 | PubMed ID:20843800 | HubMed [Wang2010]
  2. Mazurkewich S, Wang W, and Seah SY. (2014) Biochemical and structural analysis of RraA proteins to decipher their relationships with 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate aldolases. Biochemistry. 53, 542-53. DOI:10.1021/bi401486g | PubMed ID:24359411 | HubMed [Mazurkewich2014]
  3. Mazurkewich S, Brott AS, Kimber MS, and Seah SY. (2016) Structural and Kinetic Characterization of the 4-Carboxy-2-hydroxymuconate Hydratase from the Gallate and Protocatechuate 4,5-Cleavage Pathways of Pseudomonas putida KT2440. J Biol Chem. 291, 7669-86. DOI:10.1074/jbc.M115.682054 | PubMed ID:26867578 | HubMed [Mazurkewich2016]
  4. Arnling Bååth J, Mazurkewich S, Knudsen RM, Poulsen JN, Olsson L, Lo Leggio L, and Larsbrink J. (2018) Biochemical and structural features of diverse bacterial glucuronoyl esterases facilitating recalcitrant biomass conversion. Biotechnol Biofuels. 11, 213. DOI:10.1186/s13068-018-1213-x | PubMed ID:30083226 | HubMed [ArnlingBaath2018]
All Medline abstracts: PubMed | HubMed