Comparative modelling of a novel enzyme: Mus musculus leucine decarboxylase

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dc.authoridSAHUTOGLU, Arif Sercan/0000-0003-1183-3553
dc.contributor.authorSahutoglu, Arif Sercan
dc.date.accessioned2025-01-27T20:53:51Z
dc.date.available2025-01-27T20:53:51Z
dc.date.issued2020
dc.departmentÇanakkale Onsekiz Mart Üniversitesi
dc.description.abstractLeucine decarboxylase (LDC) is a recently proposed enzyme with no official enzyme commission number yet. It is encoded by the Mus musculus gene Gm853 which is expressed at kidneys, generating isopentylamine, an alkylmonoamine that has not been described to be formed by any metazoan enzyme yet. Although the relevance of LDC in mammalian physiology has not been fully determined, isopentylamine is a potential modulator which may have effects on insulin secretion and healthy gut microbiota formation. The LDC is a stable enzyme that specifically decarboxylates L-leucine but does not decarboxylate ornithine or lysine as its paralogues ornithine decarboxylase (ODC; EC: 4.1.1.17) and lysine decarboxylase (KDC; EC: 4.1.1.18) do. It does not act as an antizyme inhibitor and does not decarboxylate branched amino acids such as valine and isoleucine as it is another paralogue valine decarboxylase (VDC; EC: 4.1.1.14). The crystal structure of the enzyme has not been determined yet but there are homologous structures with complete coverage in Protein Data Bank (PDB) which makes LDC a good candidate for comparative modelling. In this study, homology models of LDC were generated and used in cofactor and substrate docking to understand the structure/function relationship underlying the unique selectivity of LDC enzyme.
dc.identifier.doi10.3906/kim-2003-63
dc.identifier.endpage832
dc.identifier.issn1300-0527
dc.identifier.issue3
dc.identifier.pmid33488196
dc.identifier.scopus2-s2.0-85090254762
dc.identifier.scopusqualityQ3
dc.identifier.startpage817
dc.identifier.trdizinid354377
dc.identifier.urihttps://doi.org/10.3906/kim-2003-63
dc.identifier.urihttps://search.trdizin.gov.tr/tr/yayin/detay/354377
dc.identifier.urihttps://hdl.handle.net/20.500.12428/25873
dc.identifier.volume44
dc.identifier.wosWOS:000538115400021
dc.identifier.wosqualityQ4
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakTR-Dizin
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherTubitak Scientific & Technological Research Council Turkey
dc.relation.ispartofTurkish Journal of Chemistry
dc.relation.publicationcategoryinfo:eu-repo/semantics/openAccess
dc.rightsinfo:eu-repo/semantics/openAccess
dc.snmzKA_WoS_20250125
dc.subjectHomology modelling
dc.subjectleucine decarboxylase
dc.subjectisopentylamine
dc.subjectGm853
dc.subjectornithine decarboxylase
dc.titleComparative modelling of a novel enzyme: Mus musculus leucine decarboxylase
dc.typeArticle

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