Abstract

Cystathionine-β-synthase (CBS) belongs to a large family of pyridoxal 5’-phosphate (PLP)-dependent enzymes, responsible for the sulfur metabolism. The heme-dependent protein CBS is part of regulatory pathways also involving the gasotransmitter hydrogen sulfide. Malfunction of CBS can lead to pathologic conditions like cancer, cardiovascular and neurodegenerative disorders. Truncation of residues 1–40, absent in X-ray structures of CBS, reduces but does not abolish the activity of the enzyme. Here we report the NMR resonance assignment and heme interaction studies for the N-terminal peptide stretch of CBS. We present NMR-spectral evidence that residues 1–40 constitute an intrinsically disordered region in CBS and interact with heme via a cysteine-proline based motif.

Details

Title
Heme interaction of the intrinsically disordered N-terminal peptide segment of human cystathionine-β-synthase
Author
Kumar, Amit 1 ; Wißbrock, Amelie 2 ; Goradia, Nishit 1 ; Bellstedt, Peter 3   VIAFID ORCID Logo  ; Ramachandran, Ramadurai 1 ; Imhof, Diana 2   VIAFID ORCID Logo  ; Ohlenschläger, Oliver 1 

1  Leibniz Institute on Aging – Fritz Lipmann Institute, Jena, Germany 
2  Pharmaceutical Biochemistry and Bioanalytics, Pharmaceutical Institute, University of Bonn, Bonn, Germany 
3  Friedrich Schiller University, Faculty of Chemistry and Earth Sciences, Jena, Germany 
Pages
1-9
Publication year
2018
Publication date
Feb 2018
Publisher
Nature Publishing Group
e-ISSN
20452322
Source type
Scholarly Journal
Language of publication
English
DOI
https://doi.org/10.1038/s41598-018-20841-z
ProQuest document ID
1995240564
Copyright
© 2018. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.