Author

K. Balbuchta

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Microbiology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:bacteria (other)· 1 Research Focus:cell type annotation· 1 Organism:human· 1 Assay:proteomics· 1

Frequent Co-Authors

A. Titz· 2 shared C. Mayer· 2 shared M. Borisova· 2 shared A. Engelbrecht· 1 shared A. L. Lovering· 1 shared I. Hottmann· 1 shared K. A. Selim· 1 shared M. Calvert· 1 shared

Activity by Year

2021-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 39 mutual co-author links

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2 shared papersMicrobiology

A. Titz

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2 papers

Recent·Most cited

NamZ1 and NamZ2 from the oral pathogen Tannerella forsythia are peptidoglycan processing exo-β-N-acetylmuramidases with distinct substrate specificity

M. Borisova, K. Balbuchta, A. L. Lovering, A. Titz, C. Mayer

This study identifies two exo-β-N-acetylmuramidases from Tannerella forsythia with distinct substrate specificities, revealing functional diversity in PGN degradation.

bioRxiv · Dec 2, 2021Microbiology

Exo-beta-N-acetylmuramidase NamZ of Bacillus subtilis is the founding member of a family of exo-lytic peptidoglycan hexosaminidases

M. Müller, M. Calvert, I. Hottmann, R. M. Kluj, T. Teufel, K. Balbuchta, A. Engelbrecht, K. A. Selim, Q. Xu, M. Borisova, A. Titz, C. Mayer

The paper identifies NamZ as an exo-{beta}-N-acetylmuramidase in Bacillus subtilis, showing its role in peptidoglycan degradation and proposing it as a founding member of a new family of hexosaminidases.

bioRxiv · Jan 10, 2021Microbiology