Lysine acetylation regulates the activity of Escherichia coli pyridoxine 5'-phosphate oxidase. 2017

Jing Gu, and Yuanyuan Chen, and Hongsen Guo, and Manluan Sun, and Mingkun Yang, and Xude Wang, and Xian'en Zhang, and Jiaoyu Deng
Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China.

NÉ›-lysine acetylation is one of the most abundant post-translational modifications in eukaryote and prokaryote. Protein acetylome of Escherichia coli has been screened using mass spectrometry (MS) technology, and many acetylated proteins have been identified, including the pyridoxine 5'-phosphate oxidase (EcPNPOx), but the biological roles played by lysine acetylation in EcPNPOx still remain unknown. In this study, EcPNPOx was firstly overexpressed and purified, and two acetylated lysine residues were identified by the subsequent liquid chromatography-tandem mass spectrometry analysis. Site-directed mutagenesis analysis demonstrated that acetylated lysine residues play important roles in the enzymatic activity and enzymatic properties of the protein. EcPNPOx could be non-enzymatically acetylated by acetyl-phosphate and deacetylated by CobB in vitro. Furthermore, enzymatic activities of acetylated and deacetylated EcPNPOx were compared in vitro, and results showed that acetylation led to a decrease of its enzymatic activity, which could be rescued by CobB deacetylation. Taken together, our data suggest that CobB modulates the enzymatic activity of EcPNPOx in vitro.

UI MeSH Term Description Entries
D008239 Lysine An essential amino acid. It is often added to animal feed. Enisyl,L-Lysine,Lysine Acetate,Lysine Hydrochloride,Acetate, Lysine,L Lysine
D011499 Protein Processing, Post-Translational Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility. Amino Acid Modification, Post-Translational,Post-Translational Modification,Post-Translational Protein Modification,Posttranslational Modification,Protein Modification, Post-Translational,Amino Acid Modification, Posttranslational,Post-Translational Amino Acid Modification,Post-Translational Modifications,Post-Translational Protein Processing,Posttranslational Amino Acid Modification,Posttranslational Modifications,Posttranslational Protein Processing,Protein Processing, Post Translational,Protein Processing, Posttranslational,Amino Acid Modification, Post Translational,Modification, Post-Translational,Modification, Post-Translational Protein,Modification, Posttranslational,Modifications, Post-Translational,Modifications, Post-Translational Protein,Modifications, Posttranslational,Post Translational Amino Acid Modification,Post Translational Modification,Post Translational Modifications,Post Translational Protein Modification,Post Translational Protein Processing,Post-Translational Protein Modifications,Processing, Post-Translational Protein,Processing, Posttranslational Protein,Protein Modification, Post Translational,Protein Modifications, Post-Translational
D011734 Pyridoxaminephosphate Oxidase An enzyme catalyzing the deamination of pyridoxaminephosphate to pyridoxal phosphate. It is a flavoprotein that also oxidizes pyridoxine-5-phosphate and pyridoxine. EC 1.4.3.5. Pyridoxinephosphate Oxidase,Pyridoxine-5-Phosphate Oxidase,Oxidase, Pyridoxaminephosphate,Oxidase, Pyridoxine-5-Phosphate,Oxidase, Pyridoxinephosphate,Pyridoxine 5 Phosphate Oxidase
D002853 Chromatography, Liquid Chromatographic techniques in which the mobile phase is a liquid. Liquid Chromatography
D004795 Enzyme Stability The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat. Enzyme Stabilities,Stabilities, Enzyme,Stability, Enzyme
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D006863 Hydrogen-Ion Concentration The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH pH,Concentration, Hydrogen-Ion,Concentrations, Hydrogen-Ion,Hydrogen Ion Concentration,Hydrogen-Ion Concentrations
D000107 Acetylation Formation of an acetyl derivative. (Stedman, 25th ed) Acetylations
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D013696 Temperature The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms. Temperatures

Related Publications

Jing Gu, and Yuanyuan Chen, and Hongsen Guo, and Manluan Sun, and Mingkun Yang, and Xude Wang, and Xian'en Zhang, and Jiaoyu Deng
November 2017, Acta biochimica et biophysica Sinica,
Jing Gu, and Yuanyuan Chen, and Hongsen Guo, and Manluan Sun, and Mingkun Yang, and Xude Wang, and Xian'en Zhang, and Jiaoyu Deng
April 2003, Biochimica et biophysica acta,
Jing Gu, and Yuanyuan Chen, and Hongsen Guo, and Manluan Sun, and Mingkun Yang, and Xude Wang, and Xian'en Zhang, and Jiaoyu Deng
May 2000, Archives of biochemistry and biophysics,
Jing Gu, and Yuanyuan Chen, and Hongsen Guo, and Manluan Sun, and Mingkun Yang, and Xude Wang, and Xian'en Zhang, and Jiaoyu Deng
October 2019, The Journal of biological chemistry,
Jing Gu, and Yuanyuan Chen, and Hongsen Guo, and Manluan Sun, and Mingkun Yang, and Xude Wang, and Xian'en Zhang, and Jiaoyu Deng
August 2016, Acta biochimica et biophysica Sinica,
Jing Gu, and Yuanyuan Chen, and Hongsen Guo, and Manluan Sun, and Mingkun Yang, and Xude Wang, and Xian'en Zhang, and Jiaoyu Deng
September 2018, Genes,
Jing Gu, and Yuanyuan Chen, and Hongsen Guo, and Manluan Sun, and Mingkun Yang, and Xude Wang, and Xian'en Zhang, and Jiaoyu Deng
August 1998, Protein expression and purification,
Jing Gu, and Yuanyuan Chen, and Hongsen Guo, and Manluan Sun, and Mingkun Yang, and Xude Wang, and Xian'en Zhang, and Jiaoyu Deng
January 2002, Journal of molecular biology,
Jing Gu, and Yuanyuan Chen, and Hongsen Guo, and Manluan Sun, and Mingkun Yang, and Xude Wang, and Xian'en Zhang, and Jiaoyu Deng
January 2021, The Journal of biological chemistry,
Jing Gu, and Yuanyuan Chen, and Hongsen Guo, and Manluan Sun, and Mingkun Yang, and Xude Wang, and Xian'en Zhang, and Jiaoyu Deng
January 2022, Frontiers in bioengineering and biotechnology,
Copied contents to your clipboard!