Monobody-mediated alteration of enzyme specificity

Nature Chemical Biology
Shun-Ichi TanakaShohei Koide

Abstract

Current methods for engineering enzymes modify enzymes themselves and require a detailed mechanistic understanding or a high-throughput assay. Here, we describe a new approach where catalytic properties are modulated with synthetic binding proteins, termed monobodies, directed to an unmodified enzyme. Using the example of a β-galactosidase from Bacillus circulans, we efficiently identified monobodies that restricted its substrates for its transgalactosylation reaction and selectively enhanced the production of small oligosaccharide prebiotics.

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Citations

Jan 17, 2017·Biochemistry·Huifang YinSander S van Leeuwen
Mar 2, 2017·Protein Science : a Publication of the Protein Society·Fern ShaShohei Koide
Oct 21, 2016·Chembiochem : a European Journal of Chemical Biology·Virginia J BruceBrian R McNaughton
Mar 9, 2017·The Journal of General Physiology·Tanmay ChavanKenton Swartz
Jan 27, 2017·Nucleic Acids Research·Andrew BowmanAndreas G Ladurner
Apr 5, 2017·Scientific Reports·Shahir S RizkAnthony A Kossiakoff
Mar 8, 2019·Interface Focus·Mounir BenkouloucheIsabelle André
May 26, 2018·Chemical Society Reviews·Louis LancasterIan Wheeldon
Jan 3, 2021·Journal of Biochemistry·Norihisa YasuiAtsuko Yamashita
Mar 30, 2017·Journal of Molecular Biology·Tim KükenshönerOliver Hantschel
Mar 4, 2021·Biotechnology and Applied Biochemistry·Ahmad MovahedpourAmir Savardashtaki
Jun 23, 2021·Nature Communications·Georgios N HatzopoulosPierre Gönczy
May 15, 2018·ACS Chemical Biology·Shun-Ichi TanakaShohei Koide
Dec 18, 2018·Chemical Reviews·Ariel L Furst, Matthew B Francis
Oct 15, 2021·Biomaterials Science·Di LiHongwei Duan

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