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MetabolomicsPolyphenolic Profiling of Plants and Edible Mushrooms to Aid Characterizing Polyphenol Oxidase Selectivity

Polyphenol oxidases are important metalloenzymes that catalyze the oxidation of polyphenols. Organisms can contain multiple isoenzymes whose possible different functionality is not understood. Moreover, their substrate preference is still unexplored, and a working hypothesis assumes their specifi...

2025-08-07 | MTBLS8782 | MetaboLights
MetabolomicsEcophysiological Study of Paraburkholderia sp. Strain 1N under Soil Solution Conditions: Dynamic Substrate Preferences and Characterization of Carbon Use Efficiency

We used time-resolved metabolic footprinting, an important technical approach used to monitor changes in extracellular compound concentrations during microbial growth, to study the order of substrate utilization (i.e., substrate preferences) and kinetics of a fast-growing soil isolate, Parabu...

2020-09-28 | MTBLS1692 | MetaboLights
ProteomicsSubstrate selectivity for semisynthetic CK2 proteins
This SuperSeries is composed of the following subset Series: GSE33149: Substrate selectivity for semisynthetic CK2 proteins with various posttranslational modifications GSE33150: Substrate selectivity for semisynthetic CK2 proteins with Pin1 Refer to individual Series
ORGANISM(S): synthetic construct 
2011-10-24 | E-GEOD-33151 | biostudies-arrayexpress
ProteomicsDistinct mechanistic, conformational and substrate selectivity profiles emerging in the evolution of high catalytic activity enzymes via parallel trajectories
Recent laboratory evolution studies have demonstrated that parallel evolutionary trajectories can lead to genetically distinct enzymes with high activity towards a non-preferred substrate. However, it is unknown whether such genetically distinct enzymes have convergent conformational dynamics and me...
ORGANISM(S): Homo sapiens (Human) 
2024-07-29 | PXD053893 | Pride
Kynureninase Enzyme Substrate Hdx Engineering 
ProteomicsSubstrate selectivity for semisynthetic CK2 proteins with Pin1
Protein Ser/Thr kinase CK2 is involved in a myriad of cellular processes including cell growth and proliferation by phosphorylating hundreds of substrates, yet the regulation process of CK2 function is poorly understood. The CK2 catalytic subunit, CK2α, is phosphorylated at Thr344 and phosphorylati...
ORGANISM(S): synthetic construct 
2011-10-24 | E-GEOD-33150 | biostudies-arrayexpress
ProteomicsSubstrate selectivity for semisynthetic CK2 proteins with Pin1
Protein Ser/Thr kinase CK2 is involved in a myriad of cellular processes including cell growth and proliferation by phosphorylating hundreds of substrates, yet the regulation process of CK2 function is poorly understood. The CK2 catalytic subunit, CK2α, is phosphorylated at Thr344 and phosphorylatio...
ORGANISM(S): Homo sapiens synthetic construct 
2011-10-25 | GSE33150 | GEO
GenomicsSubstrate selectivity of semisynthetic Akt with pSer473 or O-GlcNAcSer473
Substrate selectivity of semisynthetic Akt with pSer473 or O-GlcNAcSer473
PRJNA754137 | ENA
ProteomicsSubstrate selectivity for semisynthetic CK2 proteins with various posttranslational modifications
Protein Ser/Thr kinase CK2 is involved in a myriad of cellular processes including cell growth and proliferation by phosphorylating hundreds of substrates, yet the regulation process of CK2 function is poorly understood. The CK2 catalytic subunit, CK2α, is modified by O-GlcNAc on Ser347 proximal to...
ORGANISM(S): synthetic construct 
2011-10-24 | E-GEOD-33149 | biostudies-arrayexpress
ProteomicsSubstrate selectivity for semisynthetic CK2 proteins with various posttranslational modifications
Protein Ser/Thr kinase CK2 is involved in a myriad of cellular processes including cell growth and proliferation by phosphorylating hundreds of substrates, yet the regulation process of CK2 function is poorly understood. The CK2 catalytic subunit, CK2α, is modified by O-GlcNAc on Ser347 proximal to ...
ORGANISM(S): Homo sapiens synthetic construct 
2011-10-25 | GSE33149 | GEO
Genomicssynthetic construct
Substrate selectivity for semisynthetic CK2 proteins with Pin1
PRJNA156599 | ENA
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