Why is "Catalytic triad" trending?
Latest news, Wikipedia summary, and trend analysis.
Trend Analysis
- Ranking position: #
- Date: 2026-03-13 10:07:59
This topic has appeared in the trending rankings 1 time(s) in the past year. While it does not trend frequently, its appearance suggests a renewed or concentrated surge of public interest.
Based on Wikipedia pageviews and search interest, this topic gained significant attention on the selected date.
Trend Insight
Catalytic_triad entered the ranking for the first time today at position #. This is its highest position ever recorded.
Trend History
This topic has appeared in the English Wikipedia rankings 1 time. It first appeared on 2026-03-13 and was most recently seen on 2026-03-13.
Wikipedia Overview
A catalytic triad is a set of three coordinated amino acid residues that can be found in the active site of some enzymes. Catalytic triads are most commonly found in hydrolase and transferase enzymes. An acid-base-nucleophile triad is a common motif for generating a nucleophilic residue for covalent catalysis. The residues form a charge-relay network to polarise and activate the nucleophile, which attacks the substrate, forming a covalent intermediate which is then hydrolysed to release the product and regenerate free enzyme. The nucleophile is most commonly a serine or cysteine, but occasionally threonine or even selenocysteine. The 3D structure of the enzyme brings together the triad residues in a precise orientation, even though they may be far apart in the sequence.
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Trending Topic Today
Search Interest Perspective
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Insights into a water-mediated catalytic triad architecture in CE20 carbohydrate esterases - Nature
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A low-barrier hydrogen bond mediates antibiotic resistance in a noncanonical catalytic triad - Science | AAAS
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Crystal structures reveal a thiol protease-like catalytic triad in the C-terminal region of Pasteurella multocida toxin - PNAS
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The acid-base-nucleophile catalytic triad in ABH-fold enzymes is coordinated by a set of structural elements - PLOS
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Binding modes of prothrombin cleavage site sequences to the factor Xa catalytic triad: Insights from atomistic simulations - Science Partner Journals
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A strategic Ser/Cys exchange in the catalytic triad unlocks an acyltransferase-mediated synthesis of thioesters and tertiary amides - Nature
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‐dependent protease activity and a novel mode of enzyme activation - Springer Nature Link
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Structural and functional insights into caseinolytic proteases reveal an unprecedented regulation principle of their catalytic triad - PNAS
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The catalytic triad of rice NARROW LEAF1 involves H234 - Nature
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A low-barrier hydrogen bond mediates antibiotic resistance in a noncanonical catalytic triad - Science | AAAS
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Structure of arylamine N-acetyltransferase reveals a catalytic triad - Nature
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Direct evidence of a low barrier hydrogen bond in the catalytic triad of a Serine protease - Nature
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Identification of the Catalytic Triad of Family S46 Exopeptidases, Closely Related to Clan PA Endopeptidases - Nature
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The reaction mechanism of the Ideonella sakaiensis PETase enzyme - Nature
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A new group of glycoside hydrolase family 13 α-amylases with an aberrant catalytic triad - Nature
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Structural insight into catalytic mechanism of PET hydrolase - Nature
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Catalytic Thr or Ser Residue Modulates Structural Switches in 2-Cys Peroxiredoxin by Distinct Mechanisms - Nature
Why This Topic Is Trending
This topic has recently gained attention due to increased public interest. Search activity and Wikipedia pageviews suggest growing global engagement.
Search Interest & Related Topics
Search interest data over the past 12 months indicates that this topic periodically attracts global attention. Sudden spikes often correlate with major news events, public statements, or geopolitical developments.