Distinctive structural motifs co‐ordinate the catalytic nucleophile and the residues of the oxyanion hole in the alpha/beta‐hydrolase fold enzymes-Reference-Cited by-同舟云学术

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Distinctive structural motifs co‐ordinate the catalytic nucleophile and the residues of the oxyanion hole in the alpha/beta‐hydrolase fold enzymes

Published:2018-11-12 Issue:2 Volume:28 Page:344-364
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Dimitriou Polytimi S.¹,Denesyuk Alexander I.¹²,Nakayama Toru³,Johnson Mark S.¹,Denessiouk Konstantin¹⁴^ORCID

Affiliation:

1. Structural Bioinformatics Laboratory, Biochemistry, Faculty of Science and EngineeringÅbo Akademi University Turku 20520 Finland

2. Institute for Biological Instrumentation of the Russian Academy of Sciences Pushchino 142290 Russia

3. Tohoku University, Biomolecular Engineering Sendai Miyagi 980‐8579 Japan

4. Pharmaceutical Sciences Laboratory, Faculty of Science and Engineering, PharmacyÅbo Akademi University Turku 20520 Finland

Funder

Otto A. Malm Foundation

Tor, Joe and Pentti Borgs Memorial Fund

Åbo Akademi Doctoral Network of Informational and Structural Biology

Sigrid Juselius Foundation

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.3527

Reference105 articles.

1. α/β Hydrolase fold enzymes: the family keeps growing

2. Unveiling the functional diversity of the alpha/beta hydrolase superfamily in the plant kingdom

3. ESTHER, the database of the α/β-hydrolase fold superfamily of proteins: tools to explore diversity of functions

4. How the Same Core Catalytic Machinery Catalyzes 17 Different Reactions: the Serine-Histidine-Aspartate Catalytic Triad of α/β-Hydrolase Fold Enzymes

5. Enzymatic Activity and Protein Interactions in Alpha/Beta Hydrolase Fold Proteins: Moonlighting Versus Promiscuity

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3. The active site of the SGNH hydrolase-like fold proteins: Nucleophile–oxyanion (Nuc-Oxy) and Acid–Base zones;Current Research in Structural Biology;2024

4. Substrate‐enzyme interactions and catalytic mechanism in a novel family VI esterase with dibutyl phthalate-hydrolyzing activity;Environment International;2023-08

5. Microbiological Characterization of the Biofilms Colonizing Bioplastics in Natural Marine Conditions: A Comparison between PHBV and PLA;Microorganisms;2023-05-31

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