{"doi":"10.1042/bj2150133","title":"Dual role of a single multienzyme complex in the oxidative decarboxylation of pyruvate and branched-chain 2-oxo acids in <i>Bacillus subtilis</i>","abstract":"<jats:p>The pyruvate dehydrogenase and branched-chain 2-oxo acid dehydrogenase activities of Bacillus subtilis were found to co-purify as a single multienzyme complex. Mutants of B. subtilis with defects in the pyruvate decarboxylase (E1) and dihydrolipoamide dehydrogenase (E3) components of the pyruvate dehydrogenase complex were correspondingly affected in branched-chain 2-oxo acid dehydrogenase complex activity. Selective inhibition of the E1 or lipoate acetyltransferase (E2) components in vitro led to parallel losses in pyruvate dehydrogenase and branched-chain 2-oxo acid dehydrogenase complex activity. The pyruvate dehydrogenase and branched-chain 2-oxo acid dehydrogenase complexes of B. subtilis at the very least share many structural components, and are probably one and the same. The E3 component appeared to be identical for the pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and branched-chain 2-oxo acid dehydrogenase complexes in this organism and to be the product of a single structural gene. Long-chain branched fatty acids are thought to be essential for maintaining membrane fluidity in B. subtilis, and it was observed that the ace (pyruvate dehydrogenase complex) mutant 61142 was unable rapidly to take up acetoacetate, unlike the wild-type, indicative of a defect in membrane permeability. A single pyruvate dehydrogenase and branched-chain 2-oxo acid dehydrogenase complex can be seen as an economical means of supplying two different sets of essential metabolites.</jats:p>","journal":"Biochemical Journal","year":1983,"id":673664,"datarank":0.6329261557764161,"base_score":4.219507705176107,"endowment":4.219507705176107,"self_citation_contribution":0.6329261557764161,"citation_network_contribution":0.0,"self_endowment_contribution":0.6329261557764161,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":67,"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":1760074,"name":"J A Hodgson","orcid":null,"position":1,"is_corresponding":false},{"id":1760075,"name":"R N Perham","orcid":null,"position":2,"is_corresponding":false},{"id":1760073,"name":"P N Lowe","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Dual role of a single multienzyme complex in the oxidative decarboxylation of pyruvate and branched-chain 2-oxo acids in <i>Bacillus subtilis</i>","abstract":"<jats:p>The pyruvate dehydrogenase and branched-chain 2-oxo acid dehydrogenase activities of Bacillus subtilis were found to co-purify as a single multienzyme complex. Mutants of B. subtilis with defects in the pyruvate decarboxylase (E1) and dihydrolipoamide dehydrogenase (E3) components of the pyruvate dehydrogenase complex were correspondingly affected in branched-chain 2-oxo acid dehydrogenase complex activity. Selective inhibition of the E1 or lipoate acetyltransferase (E2) components in vitro led to parallel losses in pyruvate dehydrogenase and branched-chain 2-oxo acid dehydrogenase complex activity. The pyruvate dehydrogenase and branched-chain 2-oxo acid dehydrogenase complexes of B. subtilis at the very least share many structural components, and are probably one and the same. The E3 component appeared to be identical for the pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and branched-chain 2-oxo acid dehydrogenase complexes in this organism and to be the product of a single structural gene. Long-chain branched fatty acids are thought to be essential for maintaining membrane fluidity in B. subtilis, and it was observed that the ace (pyruvate dehydrogenase complex) mutant 61142 was unable rapidly to take up acetoacetate, unlike the wild-type, indicative of a defect in membrane permeability. A single pyruvate dehydrogenase and branched-chain 2-oxo acid dehydrogenase complex can be seen as an economical means of supplying two different sets of essential metabolites.</jats:p>","is_dataset_classified":null,"base_score":4.219507705176107,"endowment":4.219507705176107,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"6414463","pmcid":"PMC1152372","openalex_id":"https://openalex.org/W204747089","authors":[],"funders":[],"total_grants":0,"fwci":1.3618,"citation_percentile":0.75985267,"influential_citations":0,"citation_trend":[{"year":2012,"count":1},{"year":2013,"count":1},{"year":2014,"count":4},{"year":2015,"count":2},{"year":2016,"count":3},{"year":2019,"count":1},{"year":2021,"count":3},{"year":2024,"count":2}],"oa_status":"bronze","license":null,"oa_locations":[{"url":"https://portlandpress.com/biochemj/article-pdf/215/1/133/579700/bj2150133.pdf","host_type":"journal"},{"url":"https://portlandpress.com/biochemj/article-pdf/215/1/133/579700/bj2150133.pdf","host_type":"publisher"},{"url":"https://doi.org/10.1042/bj2150133","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/6414463","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/1152372","host_type":"repository"}],"fields_of_study":["Amino Acid Enzymes and Metabolism","Biochemical Acid Research Studies","Enzyme Structure and Function","3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)","Bacillus subtilis","Decarboxylation","Ketone Oxidoreductases","Kinetics","Multienzyme Complexes","Mutation","Oxidation-Reduction","Pyruvate Dehydrogenase Complex"],"mesh_terms":["Bacillus subtilis","Decarboxylation","Ketone Oxidoreductases","Kinetics","Multienzyme Complexes","Mutation","Oxidation-Reduction","Pyruvate Dehydrogenase Complex","3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)"],"keywords":["Pyruvate dehydrogenase complex","Dihydrolipoyl transacetylase","Branched-chain alpha-keto acid dehydrogenase complex","Pyruvate dehydrogenase phosphatase","Pyruvate decarboxylation","Oxoglutarate dehydrogenase complex","Biochemistry","Pyruvate dehydrogenase kinase","Pyruvate dehydrogenase lipoamide kinase isozyme 1","Oxidative decarboxylation","Dehydrogenase","Dihydrolipoamide dehydrogenase","Biology","Citric acid cycle","Chemistry","Enzyme"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Clean water and sanitation"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-16T14:08:32.361183Z","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":[]}