{"doi":"10.1021/jo035397e","title":"Synthetic Peptidoglycan Substrates for Penicillin-Binding Protein 5 of Gram-Negative Bacteria","abstract":null,"journal":"The Journal of Organic Chemistry","year":2004,"id":627758,"datarank":0.586803450814222,"base_score":3.912023005428146,"endowment":3.912023005428146,"self_citation_contribution":0.586803450814222,"citation_network_contribution":0.0,"self_endowment_contribution":0.586803450814222,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":49,"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":1624965,"name":"Maxim Suvorov","orcid":null,"position":1,"is_corresponding":false},{"id":1624966,"name":"Ken-ichiro Morio","orcid":null,"position":2,"is_corresponding":false},{"id":364756,"name":"Mijoon Lee","orcid":"0000-0001-7432-0427","position":3,"is_corresponding":false},{"id":773422,"name":"Stephen Brown","orcid":"0000-0002-2337-9717","position":4,"is_corresponding":false},{"id":389145,"name":"Sergei B. Vakulenko","orcid":"0000-0002-5327-8124","position":5,"is_corresponding":false},{"id":364759,"name":"Shahriar Mobashery","orcid":"0000-0002-7695-7883","position":6,"is_corresponding":false},{"id":735474,"name":"Dusan Hesek","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Synthetic Peptidoglycan Substrates for Penicillin-Binding Protein 5 of Gram-Negative Bacteria","abstract":"The major constituent of the bacterial cell wall, peptidoglycan, is comprised of repeating units of N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM) with an appended peptide. Penicillin-binding proteins (PBPs) are involved in the final stages of bacterial cell wall assembly. Two activities for PBPs are the cross-linking of the cell wall, carried out by dd-transpeptidases, and the dd-peptidase activity, that removes the terminal d-Ala residue from peptidoglycan. The dd-peptidase activity moderates the extent of the cell wall cross-linking. There exists a balance between the two activities that is critical for the well-being of bacterial cells. We have cloned and purified PBP5 of Escherichia coli. The membrane anchor of this protein was removed, and the enzyme was obtained as a soluble protein. Two fragments of the polymeric cell wall of Gram-negative bacteria (compounds 5 and 6) were synthesized. These molecules served as substrates for PBP5. The products of the reactions of PBP5 and compounds 5 and 6 were isolated and were shown to be d-Ala and the fragments of the substrates minus the terminal d-Ala. The kinetic parameters for these enzymic reactions were evaluated. PBP5 would appear to have the potential for turnover of as many as 1.4 million peptidoglycan strands within a single doubling time (i.e., generation) of E. coli.","is_dataset_classified":null,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"14750804","pmcid":null,"openalex_id":"https://openalex.org/W14750804","authors":[],"funders":[{"funder_name":"NIGMS NIH HHS","grant_id":"GM 61629","title":null}],"total_grants":1,"fwci":0.0,"citation_percentile":0.00120279,"influential_citations":0,"citation_trend":[],"oa_status":"closed","license":null,"oa_locations":[{"url":"https://pubs.acs.org/doi/pdf/10.1021/jo035397e","host_type":"publisher"},{"url":"http://www.koreascience.or.kr/article/ArticleFullRecord.jsp?cn=TNTNB3_2009_v11n1_1","host_type":"journal"}],"fields_of_study":["Geotechnical Engineering and Analysis","Landslides and related hazards","Geotechnical Engineering and Soil Stabilization","Bacterial Proteins","Carrier Proteins","Escherichia coli","Escherichia coli Proteins","Hexosyltransferases","Muramoylpentapeptide Carboxypeptidase","Nuclear Magnetic Resonance, Biomolecular","Penicillin-Binding Proteins","Peptide Fragments","Peptidoglycan","Peptidyl Transferases","Recombinant Proteins","Substrate Specificity"],"mesh_terms":["Escherichia coli","Muramoylpentapeptide Carboxypeptidase","Penicillin-Binding Proteins","Peptidyl Transferases","Hexosyltransferases","Peptidoglycan","Peptide Fragments","Bacterial Proteins","Escherichia coli Proteins","Carrier Proteins","Recombinant Proteins","Nuclear Magnetic Resonance, Biomolecular","Substrate Specificity"],"keywords":["Magnetic dip","Rock mass classification","Joint (building)","Geotechnical engineering","Geology","Excavation","Displacement (psychology)","Structural engineering","Engineering"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Sustainable cities and communities"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-04T18:49:02.862843Z","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":[]}