Enzyme co-localisation: Mechanisms and benefits
Open accessAbstract
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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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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- 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
- hybrid
- doi.org
- Licence
- 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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