Hauptseite > Publikationsdatenbank > Enzyme co-localisation: Mechanisms and benefits > print

001     908530
005     20230123110630.0
024 7 _ |a 10.1016/j.crchbi.2022.100031
|2 doi
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037 _ _ |a FZJ-2022-02666
082 _ _ |a 570
100 1 _ |a Kondrat, Svyatoslav
|0 P:(DE-Juel1)159264
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|e Corresponding author
245 _ _ |a Enzyme co-localisation: Mechanisms and benefits
260 _ _ |a [Amsterdam]
|c 2022
|b Elsevier B.V.
336 7 _ |a article
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336 7 _ |a ARTICLE
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336 7 _ |a Journal Article
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520 _ _ |a 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.
536 _ _ |a 2171 - Biological and environmental resources for sustainable use (POF4-217)
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588 _ _ |a Dataset connected to CrossRef, Journals: juser.fz-juelich.de
700 1 _ |a Krauss, Ulrich
|0 P:(DE-Juel1)131482
|b 1
700 1 _ |a von Lieres, Eric
|0 P:(DE-Juel1)129081
|b 2
773 _ _ |a 10.1016/j.crchbi.2022.100031
|g Vol. 2, p. 100031 -
|0 PERI:(DE-600)3103456-1
|p 100031 -
|t Current research in chemical biology
|v 2
|y 2022
|x 2666-2469
856 4 _ |u https://juser.fz-juelich.de/record/908530/files/1-s2.0-S2666246922000131-main.pdf
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909 C O |o oai:juser.fz-juelich.de:908530
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913 1 _ |a DE-HGF
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914 1 _ |y 2022
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915 _ _ |a Creative Commons Attribution-NonCommercial-NoDerivs CC BY-NC-ND 4.0
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