5G4J
Phospholyase A1RDF1 from Arthrobacter in complex with phosphoethanolamine
5G4J の概要
| エントリーDOI | 10.2210/pdb5g4j/pdb |
| 関連するPDBエントリー | 5G4I |
| 分子名称 | PUTATIVE AMINOTRANSFERASE CLASS III PROTEIN, {5-hydroxy-6-methyl-4-[(E)-{[2-(phosphonooxy)ethyl]imino}methyl]pyridin-3-yl}methyl dihydrogen phosphate, SODIUM ION, ... (4 entities in total) |
| 機能のキーワード | lyase, pyridoxal phosphate, transaminase, phospholyase |
| 由来する生物種 | ARTHROBACTER AURESCENS |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 96992.08 |
| 構造登録者 | Cuetos, A.,Tuan, A.N.,Mangas Sanchez, J.,Grogan, G. (登録日: 2016-05-13, 公開日: 2016-10-19, 最終更新日: 2024-01-10) |
| 主引用文献 | Cuetos, A.,Steffen-Munsberg, F.,Mangas Sanchez, J.,Frese, A.,Bornscheuer, U.T.,Hohne, M.,Grogan, G. Structural Basis for Phospholyase Activity of a Class III Transaminase Homologue. Chembiochem, 17:2308-2311, 2016 Cited by PubMed Abstract: 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. PubMed: 27709756DOI: 10.1002/cbic.201600482 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.87 Å) |
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