{"doi":"10.1021/jacs.7b10170","title":"Identification of a Functionally Unique Family of Penicillin-Binding Proteins","abstract":null,"journal":"Journal of the American Chemical Society","year":2017,"id":651145,"datarank":0.6591673732008659,"base_score":4.394449154672439,"endowment":4.394449154672439,"self_citation_contribution":0.6591673732008659,"citation_network_contribution":0.0,"self_endowment_contribution":0.6591673732008659,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":80,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"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":260810,"name":"Atsushi Taguchi","orcid":"0000-0003-4962-0393","position":1,"is_corresponding":false},{"id":227693,"name":"Kaitlin Schaefer","orcid":"0000-0003-4825-1389","position":2,"is_corresponding":false},{"id":302051,"name":"Daria Van Tyne","orcid":"0000-0001-7284-0103","position":3,"is_corresponding":false},{"id":424092,"name":"François Lebreton","orcid":"0000-0002-7157-5026","position":4,"is_corresponding":false},{"id":302050,"name":"Michael S. Gilmore","orcid":"0000-0001-6389-832X","position":5,"is_corresponding":false},{"id":260811,"name":"Daniel Kahne","orcid":"0000-0002-8296-1424","position":6,"is_corresponding":false},{"id":260812,"name":"Suzanne Walker","orcid":"0000-0002-0545-914X","position":7,"is_corresponding":false},{"id":329671,"name":"Michael A. Welsh","orcid":"0000-0001-8268-6285","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Identification of a Functionally Unique Family of Penicillin-Binding Proteins","abstract":"Penicillin-binding proteins (PBPs) are enzymes involved in the assembly of the bacterial cell wall, a major target for antibiotics. These proteins are classified by mass into high-molecular-weight PBPs, which are transpeptidases that form peptidoglycan cross-links, and low-molecular-weight PBPs, which are typically hydrolases. We report a functionally unique family of low-molecular-weight PBPs that act as transpeptidases rather than hydrolases, but they do not cross-link peptidoglycan. We show that these PBPs can exchange d-amino acids bearing chemical tags or affinity handles into peptidoglycan precursors, including Lipid II, enabling biochemical studies of proteins involved in cell wall assembly. We report that, in two organisms, the PBPs incorporate lysine into cellular peptidoglycan and that, further, the PBPs have the unprecedented ability to transfer the primary ε-amine of lysine to peptidoglycan.","is_dataset_classified":null,"base_score":4.394449154672439,"endowment":4.394449154672439,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"29182854","pmcid":"PMC5729098","openalex_id":"https://openalex.org/W2770310439","authors":[],"funders":[{"funder_name":"National Institute of Allergy and Infectious Diseases","grant_id":"P01AI083214","title":null},{"funder_name":"National Institute of Allergy and Infectious Diseases","grant_id":"U19AI109764","title":null},{"funder_name":"National Institute of General Medical Sciences","grant_id":"F32GM123579","title":null},{"funder_name":"National Institute of General Medical Sciences","grant_id":"R01GM76710","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM066174","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM076710","title":null}],"total_grants":6,"fwci":6.2122,"citation_percentile":0.96545829,"influential_citations":0,"citation_trend":[{"year":2018,"count":8},{"year":2019,"count":7},{"year":2020,"count":16},{"year":2021,"count":8},{"year":2022,"count":12},{"year":2023,"count":15},{"year":2024,"count":5},{"year":2025,"count":4},{"year":2026,"count":5}],"oa_status":"green","license":null,"oa_locations":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/5729098","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/5729098","host_type":"repository"},{"url":"https://pubs.acs.org/doi/pdf/10.1021/jacs.7b10170","host_type":"publisher"},{"url":"https://doi.org/10.1021/jacs.7b10170","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/29182854","host_type":"repository"},{"url":"http://europepmc.org/pmc/articles/PMC5729098","host_type":"repository"}],"fields_of_study":["Bacterial Genetics and Biotechnology","Antibiotic Resistance in Bacteria","Biochemical and Structural Characterization","Amines","Bacterial Proteins","Catalytic Domain","Cell Wall","Enterococcus faecalis","Lysine","Molecular Weight","Penicillin-Binding Proteins","Peptidoglycan","Peptidyl Transferases","Streptococcus gordonii","Uridine Diphosphate N-Acetylmuramic Acid"],"mesh_terms":["Amines","Bacterial Proteins","Cell Wall","Lysine","Molecular Weight","Peptidoglycan","Peptidyl Transferases","Enterococcus faecalis","Uridine Diphosphate N-Acetylmuramic Acid","Catalytic Domain","Penicillin-Binding Proteins","Streptococcus gordonii"],"keywords":["Peptidoglycan","Penicillin binding proteins","Lipid II","Chemistry","Biochemistry","Cell wall","Lysine","Bacterial cell structure","Glycosyltransferase","Enzyme","Penicillin","Amino acid","Antibiotics","Bacteria","Biology","Genetics"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"pfam"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-10T06:43:14.040060Z","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":[]}