Structural highlights
Publication Abstract from PubMed
PLP-dependent enzymes catalyze 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 homologs, including beta-alanine:pyruvate and gamma-amino butyrate:alpha-ketoglutarate TAs, A1RDF1 displayed no TA activity. Activity screening revealed the enzyme to possess phospholyase (E.C. 4.2.3.2) activity towards O-phosphoethanolamine (PEtN), an activity described previously for vertebrate enzymes such as human AGXT2L1, and 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 homologs that display TA activity.
Structural basis for phospholyase activity of a Class III transaminase homolog.,Cuetos A, Steffen-Munsberg F, Mangas Sanchez J, Frese A, Bornscheuer UT, Hohne M, Grogan G Chembiochem. 2016 Oct 6. doi: 10.1002/cbic.201600482. PMID:27709756[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cuetos A, Steffen-Munsberg F, Mangas Sanchez J, Frese A, Bornscheuer UT, Hohne M, Grogan G. Structural basis for phospholyase activity of a Class III transaminase homolog. Chembiochem. 2016 Oct 6. doi: 10.1002/cbic.201600482. PMID:27709756 doi:http://dx.doi.org/10.1002/cbic.201600482
