Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/360158
Type: Artigo
Title: Crystal structure of a novel xylose isomerase from streptomyces sp. F-1 revealed the presence of unique features that differ from conventional classes
Author: Miyamoto, Renan Yuji
Sousa, Amanda Silva de
Vieira, Plínio Salmazo
Melo, Ricardo Rodrigues de
Scarpassa, Josiane Aniele
Ramos, Carlos Henrique Inácio
Murakami, Mario Tyago
Ruller, Roberto
Zanphorlin, Leticia Maria
Abstract: Enzymatic isomerization is a promising strategy to solve the problem of xylose fermentation and, consequently, to leverage the production of advanced biofuels and biochemicals. In a previous work, our research group discovered a new strain of Streptomyces with great biotechnological potential due to its ability to produce a broad arsenal of enzymes related to lignocellulose degradation. We applied a multidisciplinary approach involving enzyme kinetics, biophysical methods, small angle X-ray scattering and X-ray crystallography to investigate two novel xylose isomerases, XylA1F1 and XylA2F1, from this strain. We showed that while XylA1F1 prefers to act at lower temperatures and relatively lower pH, XylA2F1 is extremely stable at higher temperatures and presents a higher turnover number. Structural analysis revealed that XylA1F1 exhibits unique properties in the active site not observed in classical XylAs from classes I and II nor in its ortholog XylA2F1. It encompasses the natural substitutions, M86A and T93K, that create an extra room for substrate accommodation and narrow the active-site entrance, respectively. Such modifications may contribute to the functional differentiation of these enzymes. We have characterized two novel xylose isomerases that display distinct functional behavior and harbor unprecedented amino-acid substitutions in the catalytic interface. Our findings contribute to a better understanding of the functional and structural aspects of xylose isomerases, which might be instrumental for the valorization of the hemicellulosic fraction of vegetal biomass
Subject: Estrutura de cristal
Country: Países Baixos
Editor: Elsevier
Rights: Fechado
Identifier DOI: 10.1016/j.bbagen.2020.129549
Address: https://www.sciencedirect.com/science/article/pii/S0304416520300398
Date Issue: 2020
Appears in Collections:IQ - Artigos e Outros Documentos
IB - Artigos e Outros Documentos

Files in This Item:
File Description SizeFormat 
000520950300002.pdf3.95 MBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.