Please use this identifier to cite or link to this item: http://223.31.159.10:8080/jspui/handle/123456789/1461
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dc.contributor.authorChatterjee, Yajnaseni-
dc.contributor.authorBhowal, Bidisha-
dc.contributor.authorGupta, Kapuganti Jagadis-
dc.contributor.authorPareek, Ashwani-
dc.contributor.authorSingla-Pareek, Sneh Lata-
dc.date.accessioned2023-04-10T07:30:36Z-
dc.date.available2023-04-10T07:30:36Z-
dc.date.issued2023-
dc.identifier.citationInternational Journal of Molecular Sciences, 24(6): 5900en_US
dc.identifier.issn1422-0067-
dc.identifier.otherhttps://doi.org/10.3390/ijms24065900-
dc.identifier.urihttps://www.mdpi.com/1422-0067/24/6/5900-
dc.identifier.urihttp://223.31.159.10:8080/jspui/handle/123456789/1461-
dc.descriptionAccepted: 2 February 2023en_US
dc.description.abstractLactate/malate dehydrogenases (Ldh/Maldh) are ubiquitous enzymes involved in the central metabolic pathway of plants and animals. The role of malate dehydrogenases in the plant system is very well documented. However, the role of its homolog L-lactate dehydrogenases still remains elusive. Though its occurrence is experimentally proven in a few plant species, not much is known about its role in rice. Therefore, a comprehensive genome-wide in silico investigation was carried out to identify all Ldh genes in model plants, rice and Arabidopsis, which revealed Ldh to be a multigene family encoding multiple proteins. Publicly available data suggest its role in a wide range of abiotic stresses such as anoxia, salinity, heat, submergence, cold and heavy metal stress, as also confirmed by our qRT-PCR analysis, especially in salinity and heavy metal mediated stresses. A detailed protein modelling and docking analysis using Schrodinger Suite reveals the presence of three putatively functional L-lactate dehydrogenases in rice, namely OsLdh3, OsLdh7 and OsLdh9. The analysis also highlights the important role of Ser-219, Gly-220 and His-251 in the active site geometry of OsLdh3, OsLdh7 and OsLdh9, respectively. In fact, these three genes have also been found to be highly upregulated under salinity, hypoxia and heavy metal mediated stresses in rice.en_US
dc.description.sponsorshipS.L.S.-P. acknowledges core grant from ICGEB. Y.C., and B.B. acknowledge research fellowships from CSIR. The funding agency played no role in the design of the study or collection, analysis and interpretation of data or in writing the manuscript. Conceptualization S.L.S.-P.; methodology S.L.S.-P., A.P.; Y.C. and B.B.; software, Y.C. and B.B.; validation Y.C., K.J.G.; formal analysis S.L.S.-P., Y.C. and B.B.; investigation Y.C., B.B., K.J.G.; data curation Y.C. and B.B.; writing—original draft preparation Y.C. and B.B.; writing—review and editing Y.C., B.B., S.L.S.-P. and A.P.; supervision S.L.S.-P. and A.P.; project administration, funding acquisition S.L.S.-P. All authors have read and agreed to the published version of the manuscript.en_US
dc.language.isoen_USen_US
dc.publisherMDPI AGen_US
dc.subjectL-lactate dehydrogenaseen_US
dc.subjectmalate dehydrogenasesen_US
dc.subjectdocking scoreen_US
dc.subjectabiotic stressen_US
dc.subjectsuperfamilyen_US
dc.titleLactate dehydrogenase superfamily in rice and Arabidopsis: Understanding the molecular evolution and structural diversityen_US
dc.typeArticleen_US
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