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Crystal structure of the feruloyl esterase from Lentilactobacillus buchneri reveals a novel homodimeric state

Ferulic acid is a common constituent of the plant cell-wall matrix where it decorates and can crosslink mainly arabinoxylans to provide structural reinforcement. Microbial feruloyl esterases (FAEs) specialize in catalyzing hydrolysis of the ester bonds between phenolic acids and sugar residues in pl...

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Autores principales: Kasmaei, Kamyar Mogodiniyai, Kalyani, Dayanand C., Reichenbach, Tom, Jiménez-Quero, Amparo, Vilaplana, Francisco, Divne, Christina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9776664/
https://www.ncbi.nlm.nih.gov/pubmed/36569051
http://dx.doi.org/10.3389/fmicb.2022.1050160
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author Kasmaei, Kamyar Mogodiniyai
Kalyani, Dayanand C.
Reichenbach, Tom
Jiménez-Quero, Amparo
Vilaplana, Francisco
Divne, Christina
author_facet Kasmaei, Kamyar Mogodiniyai
Kalyani, Dayanand C.
Reichenbach, Tom
Jiménez-Quero, Amparo
Vilaplana, Francisco
Divne, Christina
author_sort Kasmaei, Kamyar Mogodiniyai
collection PubMed
description Ferulic acid is a common constituent of the plant cell-wall matrix where it decorates and can crosslink mainly arabinoxylans to provide structural reinforcement. Microbial feruloyl esterases (FAEs) specialize in catalyzing hydrolysis of the ester bonds between phenolic acids and sugar residues in plant cell-wall polysaccharides such as arabinoxylan to release cinnamoyl compounds. Feruloyl esterases from lactic acid bacteria (LAB) have been highlighted as interesting enzymes for their potential applications in the food and pharmaceutical industries; however, there are few studies on the activity and structure of FAEs of LAB origin. Here, we report the crystal structure and biochemical characterization of a feruloyl esterase (LbFAE) from Lentilactobacillus buchneri, a LAB strain that has been used as a silage additive. The LbFAE structure was determined in the absence and presence of product (FA) and reveals a new type of homodimer association not previously observed for fungal or bacterial FAEs. The two subunits associate to restrict access to the active site such that only single FA chains attached to arabinoxylan can be accommodated, an arrangement that excludes access to FA cross-links between arabinoxylan chains. This narrow specificity is further corroborated by the observation that no FA dimers are produced, only FA, when feruloylated arabinoxylan is used as substrate. Docking of arabinofuranosyl-ferulate in the LbFAE structure highlights the restricted active site and lends further support to our hypothesis that LbFAE is specific for single FA side chains in arabinoxylan.
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spelling pubmed-97766642022-12-23 Crystal structure of the feruloyl esterase from Lentilactobacillus buchneri reveals a novel homodimeric state Kasmaei, Kamyar Mogodiniyai Kalyani, Dayanand C. Reichenbach, Tom Jiménez-Quero, Amparo Vilaplana, Francisco Divne, Christina Front Microbiol Microbiology Ferulic acid is a common constituent of the plant cell-wall matrix where it decorates and can crosslink mainly arabinoxylans to provide structural reinforcement. Microbial feruloyl esterases (FAEs) specialize in catalyzing hydrolysis of the ester bonds between phenolic acids and sugar residues in plant cell-wall polysaccharides such as arabinoxylan to release cinnamoyl compounds. Feruloyl esterases from lactic acid bacteria (LAB) have been highlighted as interesting enzymes for their potential applications in the food and pharmaceutical industries; however, there are few studies on the activity and structure of FAEs of LAB origin. Here, we report the crystal structure and biochemical characterization of a feruloyl esterase (LbFAE) from Lentilactobacillus buchneri, a LAB strain that has been used as a silage additive. The LbFAE structure was determined in the absence and presence of product (FA) and reveals a new type of homodimer association not previously observed for fungal or bacterial FAEs. The two subunits associate to restrict access to the active site such that only single FA chains attached to arabinoxylan can be accommodated, an arrangement that excludes access to FA cross-links between arabinoxylan chains. This narrow specificity is further corroborated by the observation that no FA dimers are produced, only FA, when feruloylated arabinoxylan is used as substrate. Docking of arabinofuranosyl-ferulate in the LbFAE structure highlights the restricted active site and lends further support to our hypothesis that LbFAE is specific for single FA side chains in arabinoxylan. Frontiers Media S.A. 2022-12-08 /pmc/articles/PMC9776664/ /pubmed/36569051 http://dx.doi.org/10.3389/fmicb.2022.1050160 Text en Copyright © 2022 Kasmaei, Kalyani, Reichenbach, Jiménez-Quero, Vilaplana and Divne. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Microbiology
Kasmaei, Kamyar Mogodiniyai
Kalyani, Dayanand C.
Reichenbach, Tom
Jiménez-Quero, Amparo
Vilaplana, Francisco
Divne, Christina
Crystal structure of the feruloyl esterase from Lentilactobacillus buchneri reveals a novel homodimeric state
title Crystal structure of the feruloyl esterase from Lentilactobacillus buchneri reveals a novel homodimeric state
title_full Crystal structure of the feruloyl esterase from Lentilactobacillus buchneri reveals a novel homodimeric state
title_fullStr Crystal structure of the feruloyl esterase from Lentilactobacillus buchneri reveals a novel homodimeric state
title_full_unstemmed Crystal structure of the feruloyl esterase from Lentilactobacillus buchneri reveals a novel homodimeric state
title_short Crystal structure of the feruloyl esterase from Lentilactobacillus buchneri reveals a novel homodimeric state
title_sort crystal structure of the feruloyl esterase from lentilactobacillus buchneri reveals a novel homodimeric state
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9776664/
https://www.ncbi.nlm.nih.gov/pubmed/36569051
http://dx.doi.org/10.3389/fmicb.2022.1050160
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