{"doi":"10.1021/bp0101841","title":"Purification and Identification of an\n                    <i>Escherichia</i>\n                    <i>coli</i>\n                    β‐Keto Ester Reductase as 2,5‐Diketo‐\n                    <scp>d</scp>\n                    ‐gluconate Reductase YqhE","abstract":"<jats:title>Abstract</jats:title>\n                  <jats:p>\n                    An NADPH‐dependent enzyme that reduces ethyl 2‐methylacetoacetate stereoselectively to ethyl (2\n                    <jats:italic>R</jats:italic>\n                    )‐methyl‐(3\n                    <jats:italic>S</jats:italic>\n                    )‐hydroxybutanoate was purified 730‐fold from\n                    <jats:italic>Escherichia coli</jats:italic>\n                    . The N‐terminal amino acid sequence data obtained from the purified reductase were used to search the\n                    <jats:italic>E. coli</jats:italic>\n                    genome, and a single match was found at the start of the\n                    <jats:italic>yqhE</jats:italic>\n                    open reading frame. The YqhE protein had been identified previously by Yum et al. as a 2,5‐diketo‐\n                    <jats:sc>d</jats:sc>\n                    ‐gluconate reductase on the basis of sequence similarity to other bacterial homologues [Yum, D.‐Y.; Lee, B.‐Y.; Pan, J.‐G.\n                    <jats:italic>Appl.</jats:italic>\n                    <jats:italic>Environ. Microbiol.</jats:italic>\n                    <jats:bold>1999</jats:bold>\n                    ,\n                    <jats:italic>65</jats:italic>\n                    , 3341–3346]; however, it had not been examined for β‐keto ester reductions. Our results thus link a key enzyme in the microbial production of ascorbate with stereoselective β‐keto ester reductions, two important fields in biocatalysis. The purified YqhE reductase accepts ethyl acetoacetate and a variety of 2‐substituted derivatives, and its sequence is similar to other aldose reductase superfamily members that also reduce α‐substituted β‐keto esters to\n                    <jats:italic>syn</jats:italic>\n                    ‐(2\n                    <jats:italic>R</jats:italic>\n                    ,3\n                    <jats:italic>S</jats:italic>\n                    ) alcohols.\n                  </jats:p>","journal":"Biotechnology Progress","year":2002,"id":671028,"datarank":2.4969986760279967,"base_score":3.58351893845611,"endowment":3.58351893845611,"self_citation_contribution":0.5375278407684165,"citation_network_contribution":1.9594708352595802,"self_endowment_contribution":0.5375278407684165,"citer_contribution":1.9594708352595802,"corpus_percentile":null,"corpus_rank":null,"citation_count":35,"citer_count":33,"citers_with_citation_signal":29,"citers_with_endowment":29,"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":1752940,"name":"Sonia Rodriguez","orcid":null,"position":1,"is_corresponding":false},{"id":531655,"name":"Jon D. Stewart","orcid":"0000-0003-1958-0298","position":2,"is_corresponding":false},{"id":1752939,"name":"Malgorzata Habrych","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Purification and Identification of an\n                    <i>Escherichia</i>\n                    <i>coli</i>\n                    β‐Keto Ester Reductase as 2,5‐Diketo‐\n                    <scp>d</scp>\n                    ‐gluconate Reductase YqhE","abstract":"<jats:title>Abstract</jats:title>\n                  <jats:p>\n                    An NADPH‐dependent enzyme that reduces ethyl 2‐methylacetoacetate stereoselectively to ethyl (2\n                    <jats:italic>R</jats:italic>\n                    )‐methyl‐(3\n                    <jats:italic>S</jats:italic>\n                    )‐hydroxybutanoate was purified 730‐fold from\n                    <jats:italic>Escherichia coli</jats:italic>\n                    . The N‐terminal amino acid sequence data obtained from the purified reductase were used to search the\n                    <jats:italic>E. coli</jats:italic>\n                    genome, and a single match was found at the start of the\n                    <jats:italic>yqhE</jats:italic>\n                    open reading frame. The YqhE protein had been identified previously by Yum et al. as a 2,5‐diketo‐\n                    <jats:sc>d</jats:sc>\n                    ‐gluconate reductase on the basis of sequence similarity to other bacterial homologues [Yum, D.‐Y.; Lee, B.‐Y.; Pan, J.‐G.\n                    <jats:italic>Appl.</jats:italic>\n                    <jats:italic>Environ. Microbiol.</jats:italic>\n                    <jats:bold>1999</jats:bold>\n                    ,\n                    <jats:italic>65</jats:italic>\n                    , 3341–3346]; however, it had not been examined for β‐keto ester reductions. Our results thus link a key enzyme in the microbial production of ascorbate with stereoselective β‐keto ester reductions, two important fields in biocatalysis. The purified YqhE reductase accepts ethyl acetoacetate and a variety of 2‐substituted derivatives, and its sequence is similar to other aldose reductase superfamily members that also reduce α‐substituted β‐keto esters to\n                    <jats:italic>syn</jats:italic>\n                    ‐(2\n                    <jats:italic>R</jats:italic>\n                    ,3\n                    <jats:italic>S</jats:italic>\n                    ) alcohols.\n                  </jats:p>","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":"11934293","pmcid":null,"openalex_id":null,"authors":[],"funders":[],"total_grants":0,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[],"oa_status":"closed","license":"http://onlinelibrary.wiley.com/termsAndConditions#vor","oa_locations":[{"url":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1021%2Fbp0101841","host_type":"publisher"},{"url":"https://aiche.onlinelibrary.wiley.com/doi/pdf/10.1021/bp0101841","host_type":"publisher"}],"fields_of_study":[],"mesh_terms":["Escherichia coli","NADP","Sugar Alcohol Dehydrogenases","Sensitivity and Specificity","Substrate Specificity","Oxidation-Reduction","Models, Chemical"],"keywords":[],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-16T01:03:20.710819Z","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":[]}