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Biochemical characterization and molecular insights into substrate recognition of pectin methylesterase from Phytophthora infestans
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience. KTH, School of Biotechnology (BIO), Centres, Albanova VinnExcellence Center for Protein Technology, ProNova.ORCID iD: 0000-0002-3322-8621
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience. KTH, School of Biotechnology (BIO), Centres, Albanova VinnExcellence Center for Protein Technology, ProNova. Örebro Univ, Fac Med Sci, S-70362 Örebro, Sweden..ORCID iD: 0000-0003-3514-8999
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience. KTH, School of Biotechnology (BIO), Centres, Albanova VinnExcellence Center for Protein Technology, ProNova. Flinders Univ S Australia, Coll Med & Publ Hlth, Bedford Pk Campus,Sturt Rd, Bedford Pk, SA 5042, Australia..ORCID iD: 0000-0003-2809-4160
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience. KTH, School of Biotechnology (BIO), Centres, Albanova VinnExcellence Center for Protein Technology, ProNova.ORCID iD: 0000-0003-1877-4154
2022 (English)In: Computational and Structural Biotechnology Journal, E-ISSN 2001-0370, Vol. 20, p. 6023-6032Article in journal (Refereed) Published
Abstract [en]

Pectin methylesterases (PMEs) are a class of carbohydrate-active enzymes that act on the O6-methyl ester groups of the homogalacturonan component of pectins, resulting in de-esterification of the sub-strate polymers and formation of pectate and methanol. PMEs occur in higher plants and microorgan-isms, including fungi, oomycetes, bacteria, and archaea. Microbial PMEs play a crucial role in pathogens' invasion of plant tissues. Here, we have determined the structural and functional properties of Pi-PME, a PME from the oomycete plant pathogen Phytophthora infestans. This enzyme exhibits maxi-mum activity at alkaline pH (8.5) and is active over a wide temperature range (25-50 degrees C). In silico deter-mination of the structure of Pi-PME reveals that the protein consists essentially of three parallel 8-sheets interconnected by loops that adopt an overall 8-helix organization. The loop regions in the vicinity of the active site are extended compared to plant and fungal PMEs, but they are shorter than the corresponding bacterial and insect regions. Molecular dynamic simulations revealed that Pi-PME interacts most strongly with partially de-methylated homogalacturonans, suggesting that it preferentially uses this type of sub-strates. The results are compared and discussed with other known PMEs from different organisms, high-lighting the specific features of Pi-PME.

Place, publisher, year, edition, pages
Elsevier BV , 2022. Vol. 20, p. 6023-6032
Keywords [en]
Pectin methylesterases, Phytophthora infestans, Oomycete, Potato late blight, Molecular simulation
National Category
Agricultural Science Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:kth:diva-323434DOI: 10.1016/j.csbj.2022.11.003ISI: 000904618100009PubMedID: 36382180Scopus ID: 2-s2.0-85141468223OAI: oai:DiVA.org:kth-323434DiVA, id: diva2:1732482
Note

QC 20230131

Available from: 2023-01-31 Created: 2023-01-31 Last updated: 2023-01-31Bibliographically approved

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Kumar, RajenderKumar, SanjivBulone, VincentSrivastava, Vaibhav

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