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Difference between revisions of "User:Christoph Mayer"

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* [[GH12]] ''Streptomyces lividans'' endoglucanase <cite>Sulzenbacher1997b Sulzenbacher1999</cite>
 
* [[GH12]] ''Streptomyces lividans'' endoglucanase <cite>Sulzenbacher1997b Sulzenbacher1999</cite>
 
* [[GH29]] ''Thermotoga maritima'' α-fucosidase <cite>Sulzenbacher2004</cite>
 
* [[GH29]] ''Thermotoga maritima'' α-fucosidase <cite>Sulzenbacher2004</cite>
* [[GH109]] ''Elizabethkingia meningosepticum'' α-N-acetylgalactosaminidase <cite>Liu2007</cite>
+
* [[GH171]] ''Bacillus subtilis'' and ''Tannerella forsythia''b-N-acetylmuramidase <cite>Müller2021 Borisova2022</cite>
  
 
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#Sulzenbacher1997b pmid=9440876
 
#Sulzenbacher1997b pmid=9440876
 
#Sulzenbacher1999 pmid=10200171
 
#Sulzenbacher1999 pmid=10200171
#Sulzenbacher2004 pmid=14715651
+
#Müller2021 pmid=33684445
#Liu2007 pmid=17401360
+
#Borisova2022 pmid=17401360
 
</biblio>
 
</biblio>
  
 
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<!-- Do not remove this Category tag -->
 
[[Category:Contributors|Mayer,Christoph]]
 
[[Category:Contributors|Mayer,Christoph]]

Revision as of 03:57, 17 January 2024

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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.

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She has determined the crystal structures of

  • GH7 Fusarium oxysporum endoglucanase [2, 3]
  • GH11 Bacillus pumilus xylanase
  • GH12 Streptomyces lividans endoglucanase [4, 5]
  • GH29 Thermotoga maritima α-fucosidase [6]
  • GH171 Bacillus subtilis and Tannerella forsythiab-N-acetylmuramidase [7, 8, 9]

  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 | PubMed ID:8952478 [Sulzenbacher1996]
  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+ | PubMed ID:9153432 [Sulzenbacher1997a]
  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 | PubMed ID:9440876 [Sulzenbacher1997b]
  4. Sulzenbacher G, Mackenzie LF, Wilson KS, Withers SG, Dupont C, and Davies GJ. (1999). The crystal structure of a 2-fluorocellotriosyl complex of the Streptomyces lividans endoglucanase CelB2 at 1.2 A resolution. Biochemistry. 1999;38(15):4826-33. DOI:10.1021/bi982648i | PubMed ID:10200171 [Sulzenbacher1999]
  5. üller2021 pmid=33684445

    [M]
  6. Liu QP, Sulzenbacher G, Yuan H, Bennett EP, Pietz G, Saunders K, Spence J, Nudelman E, Levery SB, White T, Neveu JM, Lane WS, Bourne Y, Olsson ML, Henrissat B, and Clausen H. (2007). Bacterial glycosidases for the production of universal red blood cells. Nat Biotechnol. 2007;25(4):454-64. DOI:10.1038/nbt1298 | PubMed ID:17401360 [Borisova2022]

All Medline abstracts: PubMed