Modification of DNA with Glucose 6-Phosphate to Examine the Glycolytic Enzyme Phosphoglucose Isomerase for DNA-amadoriase Activity

2021 ◽  
Author(s):  
Kostadin Doichev ◽  
Veselina Georgieva ◽  
Elitsa Boteva ◽  
Rumiana Mironova
Keyword(s):  
Glycolytic Enzyme ◽  
Phosphoglucose Isomerase

A New Role of Phosphoglucose Isomerase. Involvement of the Glycolytic Enzyme in Aldehyde Metabolism

2005 ◽  
Vol 70 (11) ◽  
pp. 1251-1255 ◽  
Author(s):  
Z. S. Agadjanyan ◽  
L. F. Dmitriev ◽  
S. F. Dugin
Keyword(s):  
Glycolytic Enzyme ◽  
Phosphoglucose Isomerase

Genome-wide analysis of Kluyveromyces lactis in wild-type and rag2 mutant strains

Genome ◽  
2004 ◽  
Vol 47 (5) ◽  
pp. 970-978 ◽  
Author(s):  
Manuel Becerra ◽  
Nuria Tarrío ◽  
M Isabel González-Siso ◽  
M Esperanza Cerdán
Keyword(s):  
Kluyveromyces Lactis ◽  
Glycolytic Enzyme ◽  
Pentose Phosphate ◽  
Phosphoglucose Isomerase ◽  
Transcriptional Level ◽  
Dna Arrays ◽  
Gene Coding ◽  
Genome Wide ◽  
Rag2 Gene ◽  
Interesting Alternative

The use of heterologous DNA arrays from Saccharomyces cerevisiae has been tested and revealed as a suitable tool to compare the transcriptomes of S. cerevisiae and Kluyveromyces lactis, two yeasts with notable differences in their respirofermentative metabolism. The arrays have also been applied to study the changes in the K. lactis transcriptome owing to mutation in the RAG2 gene coding for the glycolytic enzyme phosphoglucose isomerase. Comparison of the rag2 mutant growing in 2% glucose versus 2% fructose has been used as a model to elucidate the importance of transcriptional regulation of metabolic routes, which may be used to reoxidize the NADPH produced in the pentose phosphate pathway. At this transcriptional level, routes related to the oxidative stress response become an interesting alternative for NADPH use.Key words: Kluyveromyces lactis, transcription, phosphoglucose isomerase, carbohydrate use.

scholarly journals The Phosphoglucose Isomerase from the Hyperthermophilic ArchaeonPyrococcus furiosusIs a Unique Glycolytic Enzyme That Belongs to the Cupin Superfamily

2001 ◽  
Vol 276 (44) ◽  
pp. 40926-40932 ◽  
Author(s):  
Corné H. Verhees ◽  
Martijn A. Huynen ◽  
Donald E. Ward ◽  
Emile Schiltz ◽  
Willem M. de Vos ◽  
...  
Keyword(s):  
Glycolytic Enzyme ◽  
Phosphoglucose Isomerase ◽  
Cupin Superfamily

scholarly journals Tracing Putative Trafficking of the Glycolytic Enzyme Enolase via SNARE-Driven Unconventional Secretion

2012 ◽  
Vol 11 (8) ◽  
pp. 1075-1082 ◽  
Author(s):  
Natsuko Miura ◽  
Aya Kirino ◽  
Satoshi Endo ◽  
Hironobu Morisaka ◽  
Kouichi Kuroda ◽  
...  
Keyword(s):  
Secretory Pathway ◽  
Fluorescent Protein ◽  
Cell Communication ◽  
Glycolytic Enzyme ◽  
Phosphoglucose Isomerase ◽  
Cell Periphery ◽  
Knockout Mutant ◽  
Independent Manner ◽  
Content Type ◽  
Green Fluorescent

ABSTRACT Glycolytic enzymes are cytosolic proteins, but they also play important extracellular roles in cell-cell communication and infection. We used Saccharomyces cerevisiae to analyze the secretory pathway of some of these enzymes, including enolase, phosphoglucose isomerase, triose phosphate isomerase, and fructose 1,6-bisphosphate aldolase. Enolase, phosphoglucose isomerase, and an N-terminal 28-amino-acid-long fragment of enolase were secreted in a sec23 -independent manner. The enhanced green fluorescent protein (EGFP)-conjugated enolase fragment formed cellular foci, some of which were found at the cell periphery. Therefore, we speculated that an overview of the secretory pathway could be gained by investigating the colocalization of the enolase fragment with intracellular proteins. The DsRed-conjugated enolase fragment colocalized with membrane proteins at the cis -Golgi complex, nucleus, endosome, and plasma membrane, but not the mitochondria. In addition, the secretion of full-length enolase was inhibited in a knockout mutant of the intracellular SNARE protein-coding gene TLG2 . Our results suggest that enolase is secreted via a SNARE-dependent secretory pathway in S. cerevisiae .

Effect of ornidazole on fertility of male rats: inhibition of a glycolysis-related motility pattern and zona binding required for fertilization in vitro

Reproduction ◽  
2000 ◽  
pp. 127-135 ◽  
Author(s):  
W Bone ◽  
NG Jones ◽  
G Kamp ◽  
CH Yeung ◽  
TG Cooper
Keyword(s):  
Zona Pellucida ◽  
Glucose Utilization ◽  
Cumulus Cells ◽  
Glycolytic Enzyme ◽  
Male Rats ◽  
Fertilization In Vitro ◽  
Swimming Pattern ◽  
Principal Piece ◽  
Free Media

The effects of the male antifertility agent ornidazole on glycolysis as a prerequisite for fertilization were investigated in rats. Antifertility doses of ornidazole inhibited glycolysis within mature spermatozoa as determined from the lack of glucose utilization, reduced acidosis under anaerobic conditions and reduced glycolytic enzyme activity. As a consequence, cauda epididymidal spermatozoa from ornidazole-fed rats were unable to fertilize rat oocytes in vitro, with or without cumulus cells, which was not due to transfer of an inhibitor in epididymal fluid with the spermatozoa. Under IVF conditions, binding to the zona pellucida was reduced in spermatozoa from ornidazole-fed males and the spermatozoa did not undergo a change in swimming pattern, which was observed in controls. The block to fertilization could be explained by the disruption of glycolysis-dependent events, since reduced binding to the zona pellucida and a lack of kinematic changes were demonstrated by control spermatozoa in glucose-free media in the presence of respiratory substrates. The importance of glycolysis for binding to, and penetration of, the zona pellucida, and hyperactivation in rats is discussed in relation to the glycolytic production of ATP in the principal piece in which local deprivation of energy may explain the reduced force of spermatozoa from ornidazole-fed males.

Structure-Based Virtual Screening and Biochemical Evaluation for the Identification of Novel Trypanosoma brucei Aldolase Inhibitors

2018 ◽  
Vol 18 (5) ◽  
pp. 397-405 ◽  
Author(s):  
Leonardo L.G. Ferreira ◽  
Rafaela S. Ferreira ◽  
David L. Palomino ◽  
Adriano D. Andricopulo
Keyword(s):  
Drug Discovery ◽  
Virtual Screening ◽  
Trypanosoma Brucei ◽  
Enzyme Inhibitor ◽  
Practical Knowledge ◽  
Glycolytic Enzyme ◽  
Structure Based Drug Design ◽  
Biochemical Evaluation ◽  
Dynamics Simulations ◽  
Fructose 1,6 Bisphosphate

Introduction: The glycolytic enzyme fructose-1,6-bisphosphate aldolase is a validated molecular target in human African trypanosomiasis (HAT) drug discovery, a neglected tropical disease (NTD) caused by the protozoan Trypanosoma brucei. Herein, a structure-based virtual screening (SBVS) approach to the identification of novel T. brucei aldolase inhibitors is described. Distinct molecular docking algorithms were used to screen more than 500,000 compounds against the X-ray structure of the enzyme. This SBVS strategy led to the selection of a series of molecules which were evaluated for their activity on recombinant T. brucei aldolase. The effort led to the discovery of structurally new ligands able to inhibit the catalytic activity of the enzyme. Results: The predicted binding conformations were additionally investigated in molecular dynamics simulations, which provided useful insights into the enzyme-inhibitor intermolecular interactions. Conclusion: The molecular modeling results along with the enzyme inhibition data generated practical knowledge to be explored in further structure-based drug design efforts in HAT drug discovery.

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