دورية أكاديمية
أعرض في EDS

Purification and characterization of a novel medium-chain ribitol dehydrogenase from a lichen-associated bacterium Sphingomonas sp.

التفاصيل البيبلوغرافية
العنوان: Purification and characterization of a novel medium-chain ribitol dehydrogenase from a lichen-associated bacterium Sphingomonas sp.
المؤلفون: Tran KN; Department of Biomedical Science and Center for Bio-Nanomaterials, Daegu University, Gyeongsan, South Korea., Pham N; Department of Biomedical Science and Center for Bio-Nanomaterials, Daegu University, Gyeongsan, South Korea., Jang SH; Department of Biomedical Science and Center for Bio-Nanomaterials, Daegu University, Gyeongsan, South Korea., Lee C; Department of Biomedical Science and Center for Bio-Nanomaterials, Daegu University, Gyeongsan, South Korea.
المصدر: PloS one [PLoS One] 2020 Jul 08; Vol. 15 (7), pp. e0235718. Date of Electronic Publication: 2020 Jul 08 (Print Publication: 2020).
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Public Library of Science Country of Publication: United States NLM ID: 101285081 Publication Model: eCollection Cited Medium: Internet ISSN: 1932-6203 (Electronic) Linking ISSN: 19326203 NLM ISO Abbreviation: PLoS One Subsets: MEDLINE
أسماء مطبوعة: Original Publication: San Francisco, CA : Public Library of Science
مواضيع طبية MeSH: Bacterial Proteins/*isolation & purification , Bacterial Proteins/*metabolism , Lichens/*microbiology , Ribitol/*metabolism , Sphingomonas/*enzymology , Sugar Alcohol Dehydrogenases/*isolation & purification , Sugar Alcohol Dehydrogenases/*metabolism, Amino Acid Sequence ; Bacterial Proteins/genetics ; Sequence Homology ; Sphingomonas/growth & development ; Substrate Specificity ; Sugar Alcohol Dehydrogenases/genetics
مستخلص: Sugar alcohols (polyols) are abundant carbohydrates in lichen-forming algae and transported to other lichen symbionts, fungi, and bacteria. Particularly, ribitol is an abundant polyol in the lichen Cetraria sp. Polyols have important physiological roles in lichen symbiosis, but polyol utilization in lichen-associated bacteria has been largely unreported. Herein, we purified and characterized a novel ribitol dehydrogenase (RDH) from a Cetraria sp.-associated bacterium Sphingomonas sp. PAMC 26621 grown on a minimal medium containing D-ribitol (the RDH hereafter referred to as SpRDH). SpRDH is present as a trimer in its native form, and the molecular weight of SpRDH was estimated to be 39 kDa by SDS-PAGE and 117 kDa by gel filtration chromatography. SpRDH converted D-ribitol to D-ribulose using NAD+ as a cofactor. As far as we know, SpRDH is the first RDH belonging to the medium-chain dehydrogenase/reductase family. Multiple sequence alignments indicated that the catalytic amino acid residues of SpRDH consist of Cys37, His65, Glu66, and Glu157, whereas those of short-chain RDHs consist of Ser, Tyr, and Lys. Furthermore, unlike other short-chain RDHs, SpRDH did not require divalent metal ions for its catalytic activity. Despite SpRDH originating from a psychrophilic Arctic bacterium, Sphingomonas sp., it had maximum activity at 60°C and exhibited high thermal stability within the 4-50°C range. Further studies on the structure/function relationship and catalytic mechanism of SpRDH will expand our understanding of its role in lichen symbiosis.
Competing Interests: The authors have declared that no competing interests exist.
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المشرفين على المادة: 0 (Bacterial Proteins)
488-81-3 (Ribitol)
EC 1.1.- (Sugar Alcohol Dehydrogenases)
EC 1.1.1.56 (ribitol 2-dehydrogenase)
تواريخ الأحداث: Date Created: 20200709 Date Completed: 20200910 Latest Revision: 20240329
رمز التحديث: 20240329
مُعرف محوري في PubMed: PMC7343156
DOI: 10.1371/journal.pone.0235718
PMID: 32639976
قاعدة البيانات: MEDLINE
الوصف
تدمد:1932-6203
DOI:10.1371/journal.pone.0235718