Comparative modelling of a novel enzyme: Mus musculus leucine decarboxylase
Autor: | Arif Sercan Şahutoğlu |
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Jazyk: | angličtina |
Rok vydání: | 2020 |
Předmět: |
isopentylamine
Lysine decarboxylase Chemistry leucine decarboxylase Valine decarboxylase Enzyme Commission number General Chemistry Ornithine Article Gm853 Ornithine decarboxylase chemistry.chemical_compound Biochemistry Valine ornithine decarboxylase Homology modelling Leucine Homology modelling leucine decarboxylase isopentylamine Gm853 ornithine decarboxylase Ornithine decarboxylase antizyme |
Zdroj: | Turkish Journal of Chemistry Volume: 44, Issue: 3 817-832 |
ISSN: | 1303-6130 1300-0527 |
Popis: | Leucine 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. |
Databáze: | OpenAIRE |
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