Lysine acetylation of Escherichia coli lactate dehydrogenase regulates enzyme activity and lactate synthesis

Liu, Min; Huo, Meitong; Liu, Changshui; Guo, Likun; Ding, Yamei; Ma, Qingjun; Qi, Qingsheng; Xian, Ming; Zhao, Guang

doi:10.3389/fbioe.2022.966062

Cited by 8 publications

(5 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…functionality [60]. Also, it has been approved that: Lysine acetylation in Escherichia coli regulates enzyme activity and lactate synthesis [61]. The lysine acylation necessary for activating E coli, and allows the actual effects of lysine acetylation for protein productive functions [62].…”

Section: Figurementioning

confidence: 99%

Decreasing in Lysine Reflect Lysosomal Dysfunction and Accumulated Phenylalanine which Connected to WMH and CVD and Both of Phenylketonuria and Calcifications where N-Acetylcysteine Prevent Organs Failure

M El Tantawi

2024

J Cardiol Res Rev Rep

View full text Add to dashboard Cite

Phenylalanine function stabilized by lysine which found on lysosomal surface, that Phe necessary to regulate the synthesis or secretion of α-amylase, trypsin and lipase, where the Severe acute pancreatitis in a child with phenylketonuria. The phenylketonuria due to decreased lysine followed by lysosomal dysfunction that will be result of deficiency in phenylalanine function that will not form pancreatic enzymes and stomach enzyme and will be accumulated. The Lysosomal dysfunction will be result of accumulation of undigested polymer including inflammation which play important roles in pathophysiology, that reflect reduction in lysine acylation followed by reduction in aminoacyl tRNAs which promote Phe and E coli functions for activating protein and mRNAs synthesis, that will be followed by increasing in TNf-a synthesis (and reduction in VEGF-As ) which activate NK (not beings related to human immune proper function ) which regulated by the undigested polymers in random pathways stimulated by TNf-a functional pathway (activated by NLRP3 inflammasome. Retinoic acid is necessary to promote lysine acylation which regulate aminoacyl-tRNAs production regulated by mitochondrial enzymes, which regulate mRNA production by E coli (regulated by phenylalanine) that necessary to run antioxidant functions and cellular biosynthesis. Lysine acetylation so important to regulates the activity of Escherichia coli Sadenosylmethionine synthase. RNA (produced by E coli) is 2′-O-methylated demonstrated higher stability that can improve immune by promoting anti-inflammatory processes and improve myocardial functions, and adopt heart constriction by activating NR4As pathway. The antihypertensive pathway mechanism is: the Lysine ¬¬>activate ATPase (stimulate retinoic acid “RA” ) ¬¬>Lysine acetylation ¬¬> promote Phe/ hydroxylase ¬¬> followed by ¬>activate Tyr/ hydroxylase ¬>activate dopamine ¬> activate NR4As pathway ¬>GC-beta ¬>activate both of Oxytocin and Nrf2 ¬> Ang2-AT2 and VEGF-A productive functions ¬>heme oxygenase ¬>anti-inflammatory growth and processes. Lysine Methylation has important role in adopt hypertension through activating pervious Antihypertensive pathway mediated by Phe hydroxylase synthesis and Tyr hydroxylase production followed by activating both of dopamine and NR4As pathway. The oxidation of phenylalanyl-tRNA synthetase positively regulates translational quality control, and regulates the initiation of digestive enzyme mRNA translation, where consecutive AAA-lysines is paused for encoding Phe followed by ribosome sliding on homopolymeric A sequence. That lysine activates mitochondria function followed by promoting Phenylalanine and phenylalanine-tRNAs productions by translations within E coli, followed by Phe/ hydroxylase activate Tyr hydroxylase production which activate dopamine synthesis. And positively, Lysine is the most effective amino acid for activating all of ATPase, GTPase, and lysosomes, and E coli functions, where ATPase necessary for activating lysine Phosphorylation for activating lysosome digestion, followed by activating E coli through activating Phe hydroxylase production, while GTPase necessary for activating mitochondrial repairs, which act on pro-inflammation and cholesterol for activating estrogen production and activating the NR4As pathway which activate all of Oxytocin, Nrf2 followed by Ang2-AT2 and VEGF-A production and then followed by activating heme oxygenase and anti-inflammatory growth and processes that prevent LV-hypertrophy, and prevent coronary calcification.

show abstract

Section: Figurementioning

confidence: 99%

Decreasing in Lysine Reflect Lysosomal Dysfunction and Accumulated Phenylalanine which Connected to WMH and CVD and Both of Phenylketonuria and Calcifications where N-Acetylcysteine Prevent Organs Failure

M El Tantawi

2024

J Cardiol Res Rev Rep

View full text Add to dashboard Cite

show abstract

“…However, residue K9 also showed the same decrease in the acetylation levels, but its enzymatic activity increased 2.5-fold. According to the 3D-modelled structure of LdhA, K154 may be involved in binding the substrate and cofactor, while K248 and K9 are not the catalytic key sites, but both help stabilize the LdhA conformation ( Liu et al., 2022 ).…”

Section: Cellular Processes Regulated By Acetylationmentioning

confidence: 99%

Bacterial protein acetylation: mechanisms, functions, and methods for study

Rizo,

Encarnación-Guevara

2024

Front. Cell. Infect. Microbiol.

View full text Add to dashboard Cite

Lysine acetylation is an evolutionarily conserved protein modification that changes protein functions and plays an essential role in many cellular processes, such as central metabolism, transcriptional regulation, chemotaxis, and pathogen virulence. It can alter DNA binding, enzymatic activity, protein-protein interactions, protein stability, or protein localization. In prokaryotes, lysine acetylation occurs non-enzymatically and by the action of lysine acetyltransferases (KAT). In enzymatic acetylation, KAT transfers the acetyl group from acetyl-CoA (AcCoA) to the lysine side chain. In contrast, acetyl phosphate (AcP) is the acetyl donor of chemical acetylation. Regardless of the acetylation type, the removal of acetyl groups from acetyl lysines occurs only enzymatically by lysine deacetylases (KDAC). KATs are grouped into three main superfamilies based on their catalytic domain sequences and biochemical characteristics of catalysis. Specifically, members of the GNAT are found in eukaryotes and prokaryotes and have a core structural domain architecture. These enzymes can acetylate small molecules, metabolites, peptides, and proteins. This review presents current knowledge of acetylation mechanisms and functional implications in bacterial metabolism, pathogenicity, stress response, translation, and the emerging topic of protein acetylation in the gut microbiome. Additionally, the methods used to elucidate the biological significance of acetylation in bacteria, such as relative quantification and stoichiometry quantification, and the genetic code expansion tool (CGE), are reviewed.

show abstract

“…To further confirm the significance of Lys182 on the impact of TTF-1 on target gene expression, we introduced another mutation in TTF-1, substituting Lys182 with arginine (K182R). Previous studies indicated that Lys-to-arginine mutants maintain a positive charge and are incapable of being acetylated, effectively mimicking a deacetylated state of Lys [38,39]. In accordance with this, the K182R mutant of TTF-1 enhanced AgRP promoter activity (Figure 6A) and AgRP mRNA expression (Figure 6C) and diminished POMC promoter activity (Figure 6B) and POMC mRNA expression (Figure 6D), which are opposite effects to those of the K182Q mutant of TTF-1, which mimics acetylated TTF-1.…”

Section: Impact Of Lys182 Mutation On Ttf-1 Activities In Regulating ...mentioning

confidence: 99%

Sirtuin1-Mediated Deacetylation of Hypothalamic TTF-1 Contributes to the Energy Deficiency Response

Kang

Yang

Kim

et al. 2023

IJMS

View full text Add to dashboard Cite

TTF-1 stimulates appetite by regulating the expression of agouti-related peptide (AgRP) and proopiomelanocortin (POMC) genes in the hypothalamus of starving animals. However, the mechanism underlying TTF-1’s response to decreased energy levels remains elusive. Here, we provide evidence that the NAD+-dependent deacetylase, sirtuin1 (Sirt1), activates TTF-1 in response to energy deficiency. Energy deficiency leads to a twofold increase in the expression of both Sirt1 and TTF-1, leading to the deacetylation of TTF-1 through the interaction between the two proteins. The activation of Sirt1, induced by energy deficiency or resveratrol treatment, leads to a significant increase in the deacetylation of TTF-1 and promotes its nuclear translocation. Conversely, the inhibition of Sirt1 prevents these Sirt1 effects. Notably, a point mutation in a lysine residue of TTF-1 significantly disrupts its deacetylation and thus nearly completely hinders its ability to regulate AgRP and POMC gene expression. These findings highlight the importance of energy-deficiency-induced deacetylation of TTF-1 in the control of AgRP and POMC gene expression.

show abstract

Lysine acetylation of Escherichia coli lactate dehydrogenase regulates enzyme activity and lactate synthesis

Cited by 8 publications

References 39 publications

Decreasing in Lysine Reflect Lysosomal Dysfunction and Accumulated Phenylalanine which Connected to WMH and CVD and Both of Phenylketonuria and Calcifications where N-Acetylcysteine Prevent Organs Failure

Decreasing in Lysine Reflect Lysosomal Dysfunction and Accumulated Phenylalanine which Connected to WMH and CVD and Both of Phenylketonuria and Calcifications where N-Acetylcysteine Prevent Organs Failure

Bacterial protein acetylation: mechanisms, functions, and methods for study

Sirtuin1-Mediated Deacetylation of Hypothalamic TTF-1 Contributes to the Energy Deficiency Response

Contact Info

Product

Resources

About