title: Backbone resonance assignment of an insect arylalkylamine N-acetyltransferase from Bombyx mori reveals conformational heterogeneity.
abstract: Arylalkylamine N-acetyltransferases (AANATs) catalyze the transfer of an acetyl group from the acetyl-group donor, acetyl-CoA, to an arylalkylamine acceptor. Although a single AANAT has been identified in mammals, insects utilize multiple AANATs in a diverse array of biological processes. AANATs belong to the GCN5-related acetyltransferase (GNAT) superfamily of enzymes, which despite their overall very low sequence homology, are characterized by a well conserved catalytic core domain. The structural properties of many GNATs have been extensively studied by X-ray crystallography that revealed common features during the catalytic cycle. Here we report the1H,13C and15N backbone NMR resonance assignment of the 24 kDa AANAT3 from Bombyx mori (bmAANAT3) as a first step towards understanding the role of protein dynamics in the catalytic properties of AANATs. Our preliminary solution NMR studies reveal that bmAANAT3 is well-folded in solution. The P-loop, which is responsible for cofactor binding, is flexible in the free-state, while a large region of the enzyme interconverts between two distinct conformations in the slow exchange regime.
authors.affiliation: Chemistry Department, University of South Florida, Tampa, FL, 33620, USA.
authors.forename: Adam A
authors.initials: AA
authors.lastname: Aboalroub
authors.affiliation: Chemistry Department, University of South Florida, Tampa, FL, 33620, USA.
authors.forename: Ziming
authors.initials: Z
authors.lastname: Zhang
authors.affiliation: Chemistry Department, University of South Florida, Tampa, FL, 33620, USA.
authors.forename: Dimitra
authors.initials: D
authors.lastname: Keramisanou
authors.affiliation: Chemistry Department, University of South Florida, Tampa, FL, 33620, USA. igelis@usf.edu.
authors.forename: Ioannis
authors.identifier: 0000-0001-8099-003X
authors.initials: I
authors.lastname: Gelis
mesh_terms: D000818:Animals; D047068:Arylalkylamine N-Acetyltransferase / Q000737:chemistry* / Q000378:metabolism*; D055162:Biocatalysis; D012831:Bombyx / Q000201:enzymology*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation
chemical_list: D047068:Arylalkylamine N-Acetyltransferase
keywords: Acetyltransferase; Arylalkylamine; GNAT; NMR