Cold-induced aldimine bond cleavage by Tris in Bacillus subtilis alanine racemase-Reference-Cited by-同舟云学术

Cold-induced aldimine bond cleavage by Tris in Bacillus subtilis alanine racemase

Published:2019 Issue:17 Volume:17 Page:4350-4358
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Bernardo-García Noelia¹²³⁴⁵^ORCID,Sánchez-Murcia Pedro A.⁶⁷⁸⁹⁵^ORCID,Espaillat Akbar¹⁰¹¹¹²¹³¹⁴,Martínez-Caballero Siseth¹²³⁴⁵,Cava Felipe¹⁰¹¹¹²¹³¹⁴,Hermoso Juan A.¹²³⁴⁵^ORCID,Gago Federico⁶⁷⁸⁹⁵^ORCID

Affiliation:

1. Department of Crystallography and Structural Biology

2. Institute of Physical Chemistry “Rocasolano”

3. CSIC

4. 28006 Madrid

5. Spain

6. Department of Biomedical Sciences

7. “Unidad Asociada IQM-CSIC”

8. University of Alcalá

9. Madrid

10. Laboratory for Molecular Infection Medicine

11. Department of Molecular Biology

12. Umeå Centre for Microbial Research

13. Umeå University

14. 90187 Umeå

Abstract

The commonly used Tris buffer acts as a surrogate substrate and deformylates pyridoxal phosphate in a bacterial alanine racemase at subzero temperatures.

Funder

Ministerio de Ciencia e Innovación

Vetenskapsrådet

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2019/OB/C9OB00223E

Reference46 articles.

1. Structural Bioinformatics in Broad-Spectrum Racemases: A New Path in Antimicrobial Research

2. Pyridoxal Phosphate Enzymes: Mechanistic, Structural, and Evolutionary Considerations

3. The crystal structure of alanine racemase from Streptococcus pneumoniae, a target for structure-based drug design

4. Structural basis for the broad specificity of a new family of amino-acid racemases

5. Another look at the cold lability of enzymes

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