User:Christoph Mayer

Christoph Mayer obtained his diploma in chemistry from the University of Freiburg i. Br., Germany and he achieved his PhD in Microbiology under supervision of Dora M. Rast from the University of Zürich, Switzerland. With a postdoc fellowship awarded by the Swiss National Science Foundation (SNF) he moved to Vancouver, BC, Canada to work in the laboratories of Stephen G. Withers and R. Anthony J. Warren in the Chemistry Department and the Michael Smith Laboratories at the University of British Columbia (UBC). There he worked on the mechanism and function of bacterial GH3 and GH20 N-acetylglucosaminidases and on the conversion of GH1 glycosidases into glycosynthases. For his habilitation he moved to the University of Konstanz, Germany, where he discovered the MurNAc 6-phosphate lactyl ether hydrolase (MurQ enzymes), a group of enzymes related to the polysaccharide lyases but not part of the CAZy world. In 2006 he was awarded an Heisenberg fellowship of the German Research Foundation (DFG). Since 2011 he is assistant professor at the University of Tübingen, Germany, where he discovered the GH170 and GH171 exo-lytic (phospho-)N-acetylmuramidases.

Christoph Mayer and his group contributed to the following CAZy families:

• GH1 Agrobacterium sp b-glucosidase (Abg) [1, 2]
• GH3 Vibrio furnisii and Cellulomonas fimi b-N-acetylglucosaminidase [1, 2]
• GH20 Cellulomonass fimi b-N-acetylglucosaminidase [3, 4]
• GH170 Staphylococcus aureus phospho-b-N-acetylmuramidase [5]
• GH171 Bacillus subtilis and Tannerella forsythia exo-b-N-acetylmuramidase [6, 7]

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1. Sulzenbacher G, Driguez H, Henrissat B, Schülein M, and Davies GJ. (1996). Structure of the Fusarium oxysporum endoglucanase I with a nonhydrolyzable substrate analogue: substrate distortion gives rise to the preferred axial orientation for the leaving group. Biochemistry. 1996;35(48):15280-7. DOI:10.1021/bi961946h |
2. Sulzenbacher G, Schülein M, and Davies GJ. (1997). Structure of the endoglucanase I from Fusarium oxysporum: native, cellobiose, and 3,4-epoxybutyl beta-D-cellobioside-inhibited forms, at 2.3 A resolution. Biochemistry. 1997;36(19):5902-11. DOI:10.1021/bi962963+ |
3. Sulzenbacher G, Shareck F, Morosoli R, Dupont C, and Davies GJ. (1997). The Streptomyces lividans family 12 endoglucanase: construction of the catalytic cre, expression, and X-ray structure at 1.75 A resolution. Biochemistry. 1997;36(51):16032-9. DOI:10.1021/bi972407v |
5. Kluj RM, Ebner P, Adamek M, Ziemert N, Mayer C, and Borisova M. (2018). Recovery of the Peptidoglycan Turnover Product Released by the Autolysin Atl in Staphylococcus aureus Involves the Phosphotransferase System Transporter MurP and the Novel 6-phospho-N-acetylmuramidase MupG. Front Microbiol. 2018;9:2725. DOI:10.3389/fmicb.2018.02725 |
6. Müller M, Calvert M, Hottmann I, Kluj RM, Teufel T, Balbuchta K, Engelbrecht A, Selim KA, Xu Q, Borisova M, Titz A, and Mayer C. (2021). The exo-β-N-acetylmuramidase NamZ from Bacillus subtilis is the founding member of a family of exo-lytic peptidoglycan hexosaminidases. J Biol Chem. 2021;296:100519. DOI:10.1016/j.jbc.2021.100519 |
7. Borisova M, Balbuchta K, Lovering A, Titz A, and Mayer C. (2022). NamZ1 and NamZ2 from the Oral Pathogen Tannerella forsythia Are Peptidoglycan Processing Exo-β-N-Acetylmuramidases with Distinct Substrate Specificities. J Bacteriol. 2022;204(3):e0059721. DOI:10.1128/jb.00597-21 |