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ProteomicsPhosphoproteomics analysis of Pseudomonas aeruginosa with PfkA overproduction
To determined the phosphorylation sites of proteins after overproduction of PfkA in MPAO1 via pHERD20T-fpkA, and cells without overproduciton of this protein was used as a control.
ORGANISM(S): Pseudomonas aeruginosa PAO1 
2024-07-20 | PXD035424 | Pride
Pfka Phosphoproteomics Pseudomonas aeruginosa Lc-msms 
ProteomicsPhosphoproteomics analysis of Pseudomonas aeruginosa with PfkA, PfkB and PfpC overproduction
To determined the phosphorylation sites of proteins after overproduction of PfkA, PfkB and PfpC individually in PAO1 via pHERD20T-pfkA, pHERD20T-pfkB and pHERD20T-pfpC.
ORGANISM(S): Pseudomonas aeruginosa PAO1 
2024-07-20 | PXD043326 | Pride
Phosphoproteomics Pseudomonas aeruginosa Kkp 
UnknownRole of pfkA and general carbohydrate catabolism in seed colonization by Enterobacter cloacae.
Not available
S-EPMC91371 | biostudies-literature
TranscriptomicsExpression of phosphofructokinase in Neisseria meningitidis
Neisseria meningitidis serogroup B is a pathogen that can infect diverse sites within the human host. According to the N. meningitidis genomic information and experimental observations glucose can be completely catabolized through the Entner-Doudoroff pathway and the pentose phosphate pathway. The E...
ORGANISM(S): Neisseria meningitidis 
2010-06-20 | E-GEOD-18951 | biostudies-arrayexpress
UnknownFine tuning the glycolytic flux ratio of EP-bifido pathway for mevalonate production by enhancing glucose-6-phosphate dehydrogenase (Zwf) and CRISPRi suppressing 6-phosphofructose kinase (PfkA) in Escherichia coli.
Not available
S-EPMC7852082 | biostudies-literature
ProteomicsIn vivo crosslinking, cell fractionation, immunoprecipitation and MS identification of proteins crosslinked to E. coli GapA-3xFLAG
Our BATCH assay suggested that glycolytic enzymes could associate into complexes of varied stoichiometry and potentially interact with proteins outside of glycolysis, moreover, PfkA, FbaA and GapA were the top interacting proteins, showing strong interactions with both the PTS and PNPase. We constru...
ORGANISM(S): Escherichia coli 
2026-07-16 | PXD068274 | Pride
Escherichia Ms Immunoprecipitation Crosslinking 
ProteomicsChemoproteomic identification of a phosphohistidine acceptor: Insights into posttranslational regulation of glycolysis
Histidine phosphorylation is an underexplored form of protein phosphorylation. Despite the widespread existence of phosphohistidine (pHis) sites, particularly in bacteria, their phosphorylation regulation and physiological functions remain poorly understood. In this study, we developed a chemoproteo...
ORGANISM(S): Escherichia coli 
2025-05-07 | PXD053006 | Pride
Cell lysate E.coli Qexactive Lc-ms/ms 
ProteomicsChemoproteomic identification of a phosphohistidine acceptor: Insights into posttranslational regulation of glycolysis
Histidine phosphorylation is an underexplored form of protein phosphorylation. Despite the widespread existence of phosphohistidine (pHis) sites, particularly in bacteria, their phosphorylation regulation and physiological functions remain poorly understood. In this study, we developed a chemoproteo...
ORGANISM(S): Escherichia coli 
2025-05-07 | PXD056526 | Pride
Cell lysate E.coli Qexactive Lc-ms/ms 
TranscriptomicsExpression of phosphofructokinase in Neisseria meningitidis
Neisseria meningitidis serogroup B is a pathogen that can infect diverse sites within the human host. According to the N. meningitidis genomic information and experimental observations glucose can be completely catabolized through the Entner-Doudoroff pathway and the pentose phosphate pathway. The E...
ORGANISM(S): Neisseria meningitidis 
2009-11-11 | GSE18951 | GEO
UnknownOptimizing Hexose Utilization Pathways of Cupriavidus necator for Improving Growth and L-Alanine Production under Heterotrophic and Autotrophic Conditions.
Not available
S-EPMC10778655 | biostudies-literature
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