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MetabolomicsConformational gating mechanism for processive catalysis of beta(1,3) -glucans

Processive catalysis is a fundamental molecular mechanism in nature to both build and dismantle complex biological polymers such as nucleic acids, proteins and carbohydrates, underpinning a broad spectrum of biotechnological applications. Here, we uncover a processive mechanism for the breakdown ...

2026-03-02 | MTBLS13959 | MetaboLights
TranscriptomicsMIWI catalysis is required for piRNA amplification-independent LINE1 transposon silencing
This SuperSeries is composed of the following subset Series: GSE32180: MIWI catalysis is required for piRNA amplification-independent LINE1 transposon silencing [microarray] GSE32184: MIWI catalysis is required for piRNA amplification-independent LINE1 transposon silencing [deep sequencing] Refer to...
ORGANISM(S): Mus musculus 
2011-11-30 | E-GEOD-32183 | biostudies-arrayexpress
UnknownProbing the Transition State in Enzyme Catalysis by High-Pressure NMR Dynamics.
Not available
S-EPMC7063682 | biostudies-literature
UnknownElucidating structure-performance relationships in whole-cell cooperative enzyme catalysis.
Not available
S-EPMC7597743 | biostudies-literature
UnknownMultiscale simulation-guided design of enzyme bioconjugates with enhanced catalysis.
Not available
S-EPMC9784400 | biostudies-literature
UnknownEvolutionary drivers of thermoadaptation in enzyme catalysis.
Not available
S-EPMC5649376 | biostudies-literature
ProteomicsActive site tyrosine residues in human NQO1 homodimer are critical for non-synchronous enzyme catalysis at the two active sites
Human NQO1 is a flavoenzyme essential for the redox metabolization of many substances and associated with wide-impacting diseases such as cancer and Alzheimer´s. Recent X-ray crystallographic studies have proposed that a few residues at the active site of NQO1 (including Tyr126 and Tyr128) may contr...
ORGANISM(S): Homo sapiens (Human) 
2026-03-25 | PXD060224 | Pride
Enzyme kinetics Flavin Quinone oxidoreductase Hydride transfer Coenzyme specificity 
UnknownCooperative Conformational Transitions Underpin the Activation Heat Capacity in the Temperature Dependence of Enzyme Catalysis.
Not available
S-EPMC11020164 | biostudies-literature
UnknownLibGENiE - A bioinformatic pipeline for the design of information-enriched enzyme libraries.
Not available
S-EPMC10510078 | biostudies-literature
UnknownSynergistic Catalysis of Tandem Michael Addition/Enantioselective Protonation Reactions by an Artificial Enzyme.
Not available
S-EPMC8353628 | biostudies-literature
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