Cited by 19Enzyme Catalysis and ImmobilizationBiochemical and Structural CharacterizationProtein Structure and Dynamics

Enzyme co-localisation: Mechanisms and benefits

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Kondrat, Svyatoslav, Krauss, Ulrich, von Lieres, Eric·2022·Current Research in Chemical Biology

Abstract

Co-localising enzymes can drastically affect their properties, such as stability, specificity, and activity, thus influencing reaction kinetics. In this review, we present a brief overview of the main methods developed for enzyme immobilisation, co-localisation, and conjugation and discuss how and why they affect the enzyme properties. We also describe the effects emerging from bringing two sequential enzymes of a cascade reaction together, particularly if and when it speeds up reaction velocity. Furthermore, we discuss enzyme compartmentalisation, or clustering of several enzymes of a cascade, and present theoretical approaches developed to optimise synthetic enzyme clusters. We also point out the plenitude of open questions, which exist despite the enormous research effort channelled into understanding enzyme co-localisation.

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Crossref · 10.1016/j.crchbi.2022.100031

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  • For complex multi-enzyme pathways, performance depends not only on enzyme abundance but also on spatial proximity and access to substrates or cofactors.

    “This is especially relevant for complex multi-enzyme pathways, where performance depends not only on enzyme abundance but also on spatial proximity and access to substrates or cofactors [216].”

    From Cyanobacteria as a Photosynthetic Chassis for Metabolic Pathway Engineering with Heterologous Gene Expression (2026) · cites this paper as [216]

    Sections 3.5 (Substrate concentration) and 2.1 (Multi-enzyme cascades by gene fusion) support the roles of local substrate concentration and cofactor channeling. Section 5 discusses enzyme number and spatial distribution in clusters. But section 4.1 explicitly says proximity alone cannot increase steady-state cascade velocity when intermediates neither degrade nor are sequestered; the claim omits that important condition. (LLM, conf=0.87)

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Research works printed but not linked: 2

  1. Bernard, C., 1857. Sur le m ecanisme physiologique de la formation du sucre dans le foie, Compte Rendu l'Acad emie des. Sci. Paris 44 (12), 578-586. URL. https://www.scopus.com/record/display.uri?eid¼2-s2.0-27044447747& origin¼inward&txGid¼f33bf45df5af2b8f02e47de517dfba72#metrics.
  2. Niemeyer, C.M., Koehler, J., Wuerdemann, C., 2002. DNA-directed assembly of bienzymic complexes from in vivo biotinylated NAD(P)H:FMN oxidoreductase and luciferase. Chembiochem 3 (2-3), 242-5, ISSN 1439-4227 (Print) 1439-4227 (Linking). https ://www.ncbi.nlm.nih.gov/pubmed/11921405.

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Authors
Kondrat, S., Krauss, U., & von Lieres, E.
Affiliations
  • University of Stuttgart (DE)
  • Forschungszentrum Jülich (DE)
Corresponding author
Kondrat, Svyatoslav
Venue
Current Research in Chemical Biology
Publisher
Elsevier BV
Published
2022
Volume
2
Pages
100031
ISSN
2666-2469 (ISSN-L)
OpenAlex
W4281633737
Cited by
19
References
166
Citations by year
2026: 5 · 2025: 4 · 2024: 2 · 2023: 7 · 2022: 1
FWCI
1.14
Type
journal article
Language
en
Open access
Locations
  • Current Research in Chemical Biology (publishedVersion, cc-by-nc-nd)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • NCN (2017/25/B/ST3/02456)
  • ERDF (EFRE 0300097)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
enzyme immobilization, enzyme conjugation, enzyme stability, enzyme specificity, reaction kinetics, cascade reactions

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