Structural and biochemical studies on the role of active site Thr166 and Asp236 in the catalytic function of D-Serine deaminase from Salmonella typhimurium-Reference-Cited by-同舟云学术

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Structural and biochemical studies on the role of active site Thr166 and Asp236 in the catalytic function of D-Serine deaminase from Salmonella typhimurium

Published:2018-09 Issue:1 Volume:504 Page:40-45
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Deka Geeta,Bharath Sakshibeedu R.,Savithri Handanhal Subbarao^ORCID,Murthy Mathur Ramabhadrashastry Narasimha

Funder

Department of Science and Technology (DST

Department of Biotechnology (DBT

INSA

IISc and CSIR

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference22 articles.

1. Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli;Höltje;Microbiol. Mol. Biol. Rev.,1998

2. Significance of the D-serine-deaminase and D-serine metabolism of Staphylococcus saprophyticus for virulence;Korte-Berwanger;Infect. Immun.,2013

3. Uropathogenic Escherichia coli use d-serine deaminase to modulate infection of the murine urinary tract;Roesch;Mol. Microbiol.,2003

4. D-amino acids in the brain: D-serine in neurotransmission and neurodegeneration;Wolosker;FEBS J.,2008

5. Controlling reaction specificity in pyridoxal phosphate enzymes;Toney;Biochim. Biophys. Acta,2011

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