Global dynamics behind enzyme catalysis, evolution, and design


Aykac Fas B., Akbas Buz Z. E., HALİLOĞLU T.

Current Opinion in Structural Biology, cilt.94, 2025 (SCI-Expanded, Scopus)

  • Yayın Türü: Makale / Derleme
  • Cilt numarası: 94
  • Basım Tarihi: 2025
  • Doi Numarası: 10.1016/j.sbi.2025.103131
  • Dergi Adı: Current Opinion in Structural Biology
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Chemical Abstracts Core, EMBASE, INSPEC, MEDLINE
  • Boğaziçi Üniversitesi Adresli: Evet

Özet

Enzymes are inherently dynamic entities, with their functions intricately governed by the interplay between conformational dynamics - ranging from local residue fluctuations to global motions - and biochemical activity. Deciphering how such dynamics coordinate higher-order cooperativity across multiple timescales to drive catalysis remains a fundamental challenge. This mini-review highlights the role of large-scale, collective motions involving domain-level displacements and hinge-based rearrangements, which not only facilitate substrate recognition, transformation, and release, but also emerge from and propagate through multidirectional allosteric interactions. Such dynamic mechanochemical coupling reflects evolutionary memory and provides a blueprint for enzyme design innovations.