Structure of Thermococcus litoralis Δ1-pyrroline-2-carboxylate reductase in complex with NADH and L-proline

Autor:	Davide M. Ferraris, Menico Rizzi, Eugenio Ferrario, Riccardo Miggiano
Rok vydání:	2020
Předmět:	chemistry.chemical_classification biology Chemistry Reductase biology.organism_classification Cofactor Amino acid Carboxylate reductase Metabolic pathway Enzyme Biochemistry Structural Biology Dehydratase biology.protein Thermococcus litoralis
Zdroj:	Acta Crystallographica Section D Structural Biology. 76:496-505
ISSN:	2059-7983
Popis:	L-Hydroxyproline (L-Hyp) is a nonstandard amino acid that is present in certain proteins, in some antibiotics and in the cell-wall components of plants. L-Hyp is the product of the post-translational modification of protein prolines by prolyl hydroxylase enzymes, and the isomers trans-3-hydroxy-L-proline (T3LHyp) and trans-4-hydroxy-L-proline (T4LHyp) are major components of mammalian collagen. T4LHyp follows two distinct degradation pathways in bacteria and mammals, while T3LHyp is metabolized by a two-step metabolic pathway that is conserved in bacteria and mammals, which involves a T3LHyp dehydratase and a Δ1-pyrroline-2-carboxylate (Pyr2C) reductase. In order to shed light on the structure and catalysis of the enzyme involved in the second step of the T3LHyp degradation pathway, the crystal structure of Pyr2C reductase from the archaeon Thermococcus litoralis DSM 5473 complexed with NADH and L-proline is presented. The model allows the mapping of the residues involved in cofactor and product binding and represents a valid model for rationalizing the catalysis of Pyr2C reductases.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::a11c3fb012c6774a32f5b6bf2d126b21 https://doi.org/10.1107/s2059798320004866 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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