{"doi":"10.1128/aem.03449-13","title":"Molecular Characterization of a Novel\n            <i>N</i>\n            -Acetyltransferase from Chryseobacterium sp","abstract":"<jats:title>ABSTRACT</jats:title>\n          <jats:p>\n            <jats:italic>N</jats:italic>\n            -Acetyltransferase from\n            <jats:named-content content-type=\"genus-species\">Chryseobacterium</jats:named-content>\n            sp. strain 5-3B is an acetyl coenzyme A (acetyl-CoA)-dependent enzyme that catalyzes the enantioselective transfer of an acetyl group from acetyl-CoA to the amino group of\n            <jats:sc>l</jats:sc>\n            -2-phenylglycine to produce (2\n            <jats:italic>S</jats:italic>\n            )-2-acetylamino-2-phenylacetic acid. We purified the enzyme from strain 5-3B and deduced the N-terminal amino acid sequence. The gene, designated\n            <jats:italic>natA</jats:italic>\n            , was cloned with two other hypothetical protein genes; the three genes probably form a 2.5-kb operon. The deduced amino acid sequence of NatA showed high levels of identity to sequences of putative\n            <jats:italic>N</jats:italic>\n            -acetyltransferases of\n            <jats:named-content content-type=\"genus-species\">Chryseobacterium</jats:named-content>\n            spp. but not to other known arylamine and arylalkylamine\n            <jats:italic>N</jats:italic>\n            -acetyltransferases. Phylogenetic analysis indicated that NatA forms a distinct lineage from known\n            <jats:italic>N</jats:italic>\n            -acetyltransferases. We heterologously expressed recombinant NatA (rNatA) in\n            <jats:named-content content-type=\"genus-species\">Escherichia coli</jats:named-content>\n            and purified it. rNatA showed high activity for\n            <jats:sc>l</jats:sc>\n            -2-phenylglycine and its chloro- and hydroxyl-derivatives. The\n            <jats:italic>\n              K\n              <jats:sub>m</jats:sub>\n            </jats:italic>\n            and\n            <jats:italic>V</jats:italic>\n            <jats:sub>max</jats:sub>\n            values for\n            <jats:sc>l</jats:sc>\n            -2-phenylglycine were 0.145 ± 0.026 mM and 43.6 ± 2.39 μmol · min\n            <jats:sup>−1</jats:sup>\n            · mg protein\n            <jats:sup>−1</jats:sup>\n            , respectively. The enzyme showed low activity for 5-aminosalicylic acid and 5-hydroxytryptamine, which are reported as good substrates of a known arylamine\n            <jats:italic>N</jats:italic>\n            -acetyltransferase and an arylalkylamine\n            <jats:italic>N</jats:italic>\n            -acetyltransferase. rNatA had a comparatively broad acyl donor specificity, transferring acyl groups to\n            <jats:sc>l</jats:sc>\n            -2-phenylglycine and producing the corresponding 2-acetylamino-2-phenylacetic acids (relative activity with acetyl donors acetyl-CoA, propanoyl-CoA, butanoyl-CoA, pentanoyl-CoA, and hexanoyl-CoA, 100:108:122:10:&lt;1).\n          </jats:p>","journal":"Applied and Environmental Microbiology","year":2014,"id":15263,"datarank":0.40055136481748277,"base_score":1.791759469228055,"endowment":1.791759469228055,"self_citation_contribution":0.26876392038420827,"citation_network_contribution":0.1317874444332745,"self_endowment_contribution":0.26876392038420827,"citer_contribution":0.1317874444332745,"corpus_percentile":null,"corpus_rank":null,"citation_count":5,"citer_count":4,"citers_with_citation_signal":4,"citers_with_endowment":4,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":117179,"name":"Kenji Yoshida","orcid":"0000-0003-4755-5807","position":1,"is_corresponding":false},{"id":117180,"name":"Kosei Tanaka","orcid":null,"position":2,"is_corresponding":false},{"id":117181,"name":"Ken-ichi Yoshida","orcid":null,"position":3,"is_corresponding":false},{"id":117178,"name":"Shinji Takenaka","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":1.791759469228055,"endowment":1.791759469228055,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"24375143","pmcid":"PMC3957623","openalex_id":"https://openalex.org/W2108011157","authors":[],"funders":[],"total_grants":0,"fwci":0.2002,"citation_percentile":0.65610211,"influential_citations":0,"citation_trend":[{"year":2016,"count":1},{"year":2017,"count":1},{"year":2020,"count":1},{"year":2025,"count":2}],"oa_status":"bronze","license":"https://journals.asm.org/non-commercial-tdm-license","oa_locations":[{"url":"https://aem.asm.org/content/aem/80/5/1770.full.pdf","host_type":"journal"},{"url":"https://aem.asm.org/content/aem/80/5/1770.full.pdf","host_type":"GREEN"},{"url":"https://aem.asm.org/content/aem/80/5/1770.full.pdf","host_type":"publisher"},{"url":"https://journals.asm.org/doi/pdf/10.1128/AEM.03449-13","host_type":"publisher"},{"url":"https://doi.org/10.1128/aem.03449-13","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/24375143","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/3957623","host_type":"repository"}],"fields_of_study":["Amino Acid Enzymes and Metabolism","Enzyme Structure and Function","Microbial Metabolic Engineering and Bioproduction","Chemistry","Biology","Medicine","Acetyl Coenzyme A","Acetyltransferases","Chryseobacterium","Cloning, Molecular","DNA, Bacterial","Escherichia coli","Gene Expression","Glycine","Kinetics","Molecular Sequence Data","Phenylacetates","Phylogeny","Recombinant Proteins","Sequence Analysis, DNA","Sequence Homology, Amino Acid","Substrate Specificity"],"mesh_terms":["Acetyl Coenzyme A","Acetyltransferases","Cloning, Molecular","DNA, Bacterial","Escherichia coli","Glycine","Kinetics","Molecular Sequence Data","Phenylacetates","Phylogeny","Recombinant Proteins","Substrate Specificity","Gene Expression","Sequence Homology, Amino Acid","Sequence Analysis, DNA","Chryseobacterium"],"keywords":["Chryseobacterium","Acetyltransferases","Acetyltransferase","N-acetyltransferase","Biochemistry","Phenylacetic acid","Escherichia coli","Amino acid","Peptide sequence","Enzyme","Chemistry","Biology","Stereochemistry","Gene","Acetylation","16S ribosomal RNA"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"gen"},{"name":"uniprot"},{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-06-01T17:02:57.256068Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}