Current Advances on Structure-Function Relationships of Pyridoxal 5'-Phosphate-Dependent Enzymes

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dc.contributor.authorLiang, Jingen
dc.contributor.authorHan, Qianen
dc.contributor.authorTan, Yangen
dc.contributor.authorDing, Haizhenen
dc.contributor.authorLi, Jianyongen
dc.contributor.departmentBiochemistryen
dc.date.accessioned2019-10-25T12:59:35Zen
dc.date.available2019-10-25T12:59:35Zen
dc.date.issued2019-03-05en
dc.description.abstractPyridoxal 5'-phosphate (PLP) functions as a coenzyme in many enzymatic processes, including decarboxylation, deamination, transamination, racemization, and others. Enzymes, requiring PLP, are commonly termed PLP-dependent enzymes, and they are widely involved in crucial cellular metabolic pathways in most of (if not all) living organisms. The chemical mechanisms for PLP-mediated reactions have been well elaborated and accepted with an emphasis on the pure chemical steps, but how the chemical steps are processed by enzymes, especially by functions of active site residues, are not fully elucidated. Furthermore, the specific mechanism of an enzyme in relation to the one for a similar class of enzymes seems scarcely described or discussed. This discussion aims to link the specific mechanism described for the individual enzyme to the same types of enzymes from different species with aminotransferases, decarboxylases, racemase, aldolase, cystathionine beta-synthase, aromatic phenylacetaldehyde synthase, et al. as models. The structural factors that contribute to the reaction mechanisms, particularly active site residues critical for dictating the reaction specificity, are summarized in this review.en
dc.description.notesThis work was supported by Department of Biochemistry and College of Agriculture and Life Science at Virginia Tech and US Department of Agriculture, and Natural Science Foundation of China, 31472186.en
dc.description.sponsorshipDepartment of Biochemistry at Virginia Tech; College of Agriculture and Life Science at Virginia Tech; Department of Biochemistry at US Department of Agriculture; Natural Science Foundation of ChinaNational Natural Science Foundation of China [31472186]; College of Agriculture and Life Science at US Department of Agricultureen
dc.format.mimetypeapplication/pdfen
dc.identifier.doihttps://doi.org/10.3389/fmolb.2019.00004en
dc.identifier.eissn2296-889Xen
dc.identifier.other4en
dc.identifier.pmid30891451en
dc.identifier.urihttp://hdl.handle.net/10919/95056en
dc.identifier.volume6en
dc.language.isoenen
dc.publisherFrontiersen
dc.rightsCreative Commons Attribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.subjectpyridoxal 5 '-phosphateen
dc.subjectstructure-function relationshipen
dc.subjectreaction mechanismen
dc.subjectamino acid residuesen
dc.subjectreaction specificityen
dc.titleCurrent Advances on Structure-Function Relationships of Pyridoxal 5'-Phosphate-Dependent Enzymesen
dc.title.serialFrontiers in Molecular Biosciencesen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten

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