Structural Basis for Phospholyase Activity of a Class III Transaminase Homologue
Autor: | Anibal Cuetos, Juan Mangas Sanchez, Matthias Höhne, Gideon Grogan, Uwe T. Bornscheuer, Fabian Steffen-Munsberg, Amina Frese |
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Rok vydání: | 2016 |
Předmět: |
0301 basic medicine
Aldimine Stereochemistry Class iii Molecular Dynamics Simulation Biology Biochemistry Enzyme catalysis Transaminase 03 medical and health sciences chemistry.chemical_compound Catalytic Domain Humans Transferase Arthrobacter Pyridoxal phosphate Molecular Biology Transaminases chemistry.chemical_classification Binding Sites 030102 biochemistry & molecular biology Organic Chemistry Lyase 030104 developmental biology Enzyme chemistry Pyridoxal Phosphate Biocatalysis Molecular Medicine |
Zdroj: | ChemBioChem. 17:2308-2311 |
ISSN: | 1439-4227 |
Popis: | Pyridoxal-phosphate (PLP)-dependent enzymes catalyse a remarkable diversity of chemical reactions in nature. A1RDF1 from Arthrobacter aurescens TC1 is a fold type I, PLP-dependent enzyme in the class III transaminase (TA) subgroup. Despite sharing 28 % sequence identity with its closest structural homologues, including β-alanine:pyruvate and γ-aminobutyrate:α-ketoglutarate TAs, A1RDF1 displayed no TA activity. Activity screening revealed that the enzyme possesses phospholyase (E.C. 4.2.3.2) activity towards O-phosphoethanolamine (PEtN), an activity described previously for vertebrate enzymes such as human AGXT2L1, enzymes for which no structure has yet been reported. In order to shed light on the distinctive features of PLP-dependent phospholyases, structures of A1RDF1 in complex with PLP (internal aldimine) and PLP⋅PEtN (external aldimine) were determined, revealing the basis of substrate binding and the structural factors that distinguish the enzyme from class III homologues that display TA activity. |
Databáze: | OpenAIRE |
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