RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/33682300http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/33682300http://www.w3.org/2000/01/rdf-schema#comment"Serotonin N-acetyltransferase (SNAT) is the key rate-limiting enzyme in melatonin biosynthesis. It mediates melatonin biosynthesis in plants by using serotonin and 5-methoxytryptamine (5-MT), but little is known of its underlying mechanisms. Herein, we present a detailed reaction mechanism of a SNAT from Oryza sativa through combined structural and molecular dynamics (MD) analysis. We report the crystal structures of plant SNAT in the apo and binary/ternary complex forms with acetyl-CoA (AcCoA), serotonin, and 5-MT. OsSNAT exhibits a unique enzymatically active dimeric fold not found in the known structures of arylalkylamine N-acetyltransferase (AANAT) family. The key residues W188, D189, D226, N220, and Y233 located around the active pocket are important in catalysis, confirmed by site-directed mutagenesis. Combined with MD simulations, we hypothesize a novel plausible catalytic mechanism in which D226 and Y233 function as catalytic base and acid during the acetyl-transfer reaction."xsd:string
http://purl.uniprot.org/citations/33682300http://purl.org/dc/terms/identifier"doi:10.1002/anie.202100992"xsd:string
http://purl.uniprot.org/citations/33682300http://purl.uniprot.org/core/author"Chen X."xsd:string
http://purl.uniprot.org/citations/33682300http://purl.uniprot.org/core/author"Guo Y."xsd:string
http://purl.uniprot.org/citations/33682300http://purl.uniprot.org/core/author"Liu B."xsd:string
http://purl.uniprot.org/citations/33682300http://purl.uniprot.org/core/author"Liu X."xsd:string
http://purl.uniprot.org/citations/33682300http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/33682300http://purl.uniprot.org/core/author"Xu Y."xsd:string
http://purl.uniprot.org/citations/33682300http://purl.uniprot.org/core/author"Zhou Y."xsd:string
http://purl.uniprot.org/citations/33682300http://purl.uniprot.org/core/author"Zhao Y."xsd:string
http://purl.uniprot.org/citations/33682300http://purl.uniprot.org/core/author"Liao L."xsd:string
http://purl.uniprot.org/citations/33682300http://purl.uniprot.org/core/author"Zeng Z."xsd:string
http://purl.uniprot.org/citations/33682300http://purl.uniprot.org/core/date"2021"xsd:gYear
http://purl.uniprot.org/citations/33682300http://purl.uniprot.org/core/name"Angew Chem Int Ed Engl"xsd:string
http://purl.uniprot.org/citations/33682300http://purl.uniprot.org/core/pages"12020-12026"xsd:string
http://purl.uniprot.org/citations/33682300http://purl.uniprot.org/core/title"Structural and Molecular Dynamics Analysis of Plant Serotonin N-Acetyltransferase Reveal an Acid/Base-Assisted Catalysis in Melatonin Biosynthesis."xsd:string
http://purl.uniprot.org/citations/33682300http://purl.uniprot.org/core/volume"60"xsd:string
http://purl.uniprot.org/citations/33682300http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/33682300
http://purl.uniprot.org/citations/33682300http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/33682300
http://purl.uniprot.org/uniprot/#_Q5KQI6-mappedCitation-33682300http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33682300
http://purl.uniprot.org/uniprot/Q5KQI6http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/33682300