Properties and mechanism of d -glucosaminate-6-phosphate ammonia-lyase: An aminotransferase family enzyme with d -amino acid specificity-Reference-Cited by-同舟云学术

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Properties and mechanism of d -glucosaminate-6-phosphate ammonia-lyase: An aminotransferase family enzyme with d -amino acid specificity

Published:2018-07 Issue:7 Volume:1866 Page:799-805
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Phillips Robert S.,Ting Samuel C.,Tetsadjio Ange G.,Anderson Kaitlin L.,Friez Kyle M.,Miller Katherine A.,Hoover Timothy R.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference28 articles.

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2. Correlations between carbon metabolism and virulence in bacteria;Poncet;Contrib. Microbiol.,2009

3. Genome scale reconstruction of a Salmonella metabolic model: comparison of similarity and differences with a commensal Escherichia coli strain;AbuOun;J. Biol. Chem.,2009

4. Salmonella modulates metabolism during growth under conditions that induce expression of virulence genes;Kim;Mol. BioSyst.,2013

5. Constraint-based analysis of metabolic capacity of Salmonella typhimurium during host-pathogen interaction;Raghunathan;BMC Syst. Biol.,2009

Cited by 5 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Mannose antagonizes GSDME-mediated pyroptosis through AMPK activated by metabolite GlcNAc-6P;Cell Research;2023-07-17

2. His‐163 is a stereospecific proton donor in the mechanism of d ‐glucosaminate‐6‐phosphate ammonia‐lyase;FEBS Letters;2022-08-29

3. Structure and Mechanism of d-Glucosaminate-6-phosphate Ammonia-lyase: A Novel Octameric Assembly for a Pyridoxal 5′-Phosphate-Dependent Enzyme, and Unprecedented Stereochemical Inversion in the Elimination Reaction of a d-Amino Acid;Biochemistry;2021-05-05

4. Bibliography;Biological Chirality;2020

5. The ammonia-lyases: enzymes that use a wide range of approaches to catalyze the same type of reaction;Critical Reviews in Biochemistry and Molecular Biology;2019-11-02

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