Literature DB >> 34813066

In Silico Engineering of Enzyme Access Tunnels.

Alfonso Gautieri1, Federica Rigoldi2, Archimede Torretta3, Alberto Redaelli2, Emilio Parisini4,5.   

Abstract

Enzyme engineering is a tailoring process that allows the modification of naturally occurring enzymes to provide them with improved catalytic efficiency, stability, or specificity. By introducing partial modifications to their sequence and to their structural features, enzyme engineering can transform natural enzymes into more efficient, specific and resistant biocatalysts and render them suitable for virtually countless industrial processes. Current enzyme engineering methods mostly target the active site of the enzyme, where the catalytic reaction takes place. Nonetheless, the tunnel that often connects the surface of an enzyme with its buried active site plays a key role in the activity of the enzyme as it acts as a gatekeeper and regulates the access of the substrate to the catalytic pocket. Hence, there is an increasing interest in targeting the sequence and the structure of substrate entrance tunnels in order to fine-tune enzymatic activity, regulate substrate specificity, or control reaction promiscuity.In this chapter, we describe the use of a rational in silico design and screening method to engineer the access tunnel of a fructosyl peptide oxidase with the aim to facilitate access to its catalytic site and to expand its substrate range. Our goal is to engineer this class of enzymes in order to utilize them for the direct detection of glycated proteins in diabetes monitoring devices. The design strategy involves remodeling of the backbone structure of the enzyme , a feature that is not possible with conventional enzyme engineering techniques such as single-point mutagenesis and that is highly unlikely to occur using a directed evolution approach.The proposed strategy, which results in a significant reduction in cost and time for the experimental production and characterization of candidate enzyme variants, represents a promising approach to the expedited identification of novel and improved enzymes. Rational enzyme design aims to provide in silico strategies for the fast, accurate, and inexpensive development of biocatalysts that can meet the needs of multiple industrial sectors, thus ultimately promoting the use of green chemistry and improving the efficiency of chemical processes.
© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

Entities:  

Keywords:  Access tunnel; Molecular modeling; Protein design; Rational enzyme engineering; Substrate entry

Mesh:

Year:  2022        PMID: 34813066     DOI: 10.1007/978-1-0716-1826-4_11

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  17 in total

1.  Crystal structure of the deglycating enzyme Amadoriase I in its free form and substrate-bound complex.

Authors:  Federica Rigoldi; Alfonso Gautieri; Andrea Dalle Vedove; Anna Paola Lucarelli; Simone Vesentini; Emilio Parisini
Journal:  Proteins       Date:  2016-03-16

2.  Kinetic studies, mechanism, and substrate specificity of amadoriase I from Aspergillus sp.

Authors:  X Wu; B A Palfey; V V Mossine; V M Monnier
Journal:  Biochemistry       Date:  2001-10-30       Impact factor: 3.162

3.  Structural basis of the substrate specificity of the FPOD/FAOD family revealed by fructosyl peptide oxidase from Eupenicillium terrenum.

Authors:  Weiqiong Gan; Feng Gao; Keke Xing; Minze Jia; Haiping Liu; Weimin Gong
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2015-03-20       Impact factor: 1.056

4.  Engineering fructosyl peptide oxidase to improve activity toward the fructosyl hexapeptide standard for HbA1c measurement.

Authors:  Stefano Ferri; Yusuke Miyamoto; Akane Sakaguchi-Mikami; Wakako Tsugawa; Koji Sode
Journal:  Mol Biotechnol       Date:  2013-07       Impact factor: 2.695

5.  Active site analysis of fructosyl amine oxidase using homology modeling and site-directed mutagenesis.

Authors:  Seiji Miura; Stefano Ferri; Wakako Tsugawa; Seungsu Kim; Koji Sode
Journal:  Biotechnol Lett       Date:  2006-10-17       Impact factor: 2.461

6.  Molecular dynamics simulations provide insights into the substrate specificity of FAOX family members.

Authors:  Federica Rigoldi; Ludovica Spero; Andrea Dalle Vedove; Alberto Redaelli; Emilio Parisini; Alfonso Gautieri
Journal:  Mol Biosyst       Date:  2016-07-19

7.  Crystal structure of the deglycating enzyme fructosamine oxidase (amadoriase II).

Authors:  François Collard; Jianye Zhang; Ina Nemet; Kaustubha R Qanungo; Vincent M Monnier; Vivien C Yee
Journal:  J Biol Chem       Date:  2008-07-30       Impact factor: 5.157

8.  Development of fructosyl amine oxidase specific to fructosyl valine by site-directed mutagenesis.

Authors:  Seiji Miura; Stefano Ferri; Wakako Tsugawa; Seungsu Kim; Koji Sode
Journal:  Protein Eng Des Sel       Date:  2008-01-31       Impact factor: 1.650

9.  Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega.

Authors:  Fabian Sievers; Andreas Wilm; David Dineen; Toby J Gibson; Kevin Karplus; Weizhong Li; Rodrigo Lopez; Hamish McWilliam; Michael Remmert; Johannes Söding; Julie D Thompson; Desmond G Higgins
Journal:  Mol Syst Biol       Date:  2011-10-11       Impact factor: 11.429

10.  Creation of haemoglobin A1c direct oxidase from fructosyl peptide oxidase by combined structure-based site specific mutagenesis and random mutagenesis.

Authors:  Noriyuki Ogawa; Takehide Kimura; Fumi Umehara; Yuki Katayama; Go Nagai; Keiko Suzuki; Kazuo Aisaka; Yukie Maruyama; Takafumi Itoh; Wataru Hashimoto; Kousaku Murata; Michio Ichimura
Journal:  Sci Rep       Date:  2019-01-30       Impact factor: 4.379

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