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Results 1 - 10 of 23 > >>
EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Show all pathways known for 1.8.1.14Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.14764212 Characterization and X-ray structure of the NADH-dependent coenzyme A disulfide reductase from Thermus thermophilus Biochim. Biophys. Acta Bioenerg. 1860 148080 2019 Thermus thermophilus 31520616
Show all pathways known for 1.8.1.14Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.14764212 Characterization and X-ray structure of the NADH-dependent coenzyme A disulfide reductase from Thermus thermophilus Biochim. Biophys. Acta Bioenerg. 1860 148080 2019 Thermus thermophilus ATCC BAA-163 31520616
Show all pathways known for 1.8.1.14Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.14744312 Structure and substrate specificity of the pyrococcal coenzyme A disulfide reductases/polysulfide reductases (CoADR/Psr). Implications for S(0)-based respiration and a sulfur-dependent antioxidant system in Pyrococcus Biochemistry 52 2764-2773 2013 Pyrococcus horikoshii 23530771
Show all pathways known for 1.8.1.14Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.14744312 Structure and substrate specificity of the pyrococcal coenzyme A disulfide reductases/polysulfide reductases (CoADR/Psr). Implications for S(0)-based respiration and a sulfur-dependent antioxidant system in Pyrococcus Biochemistry 52 2764-2773 2013 Pyrococcus horikoshii OT-3 23530771
Show all pathways known for 1.8.1.14Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.14764676 A broader active site in Pyrococcus horikoshii CoA disulfide reductase accommodates larger substrates and reveals evidence of subunit asymmetry FEBS open bio 8 1083-1092 2018 Pyrococcus horikoshii 29988575
Show all pathways known for 1.8.1.14Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.14764676 A broader active site in Pyrococcus horikoshii CoA disulfide reductase accommodates larger substrates and reveals evidence of subunit asymmetry FEBS open bio 8 1083-1092 2018 Pyrococcus horikoshii ATCC 700860 29988575
Show all pathways known for 1.8.1.14Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.14394071 Levels of acetyl coenzyme A, reduced and oxidized coenzyme A, and coenzyme A in disulfide linkage to protein in dormant germinated spores and growing and sporulating cells of Bacillus megaterium J. Bacteriol. 132 444-452 1979 Priestia megaterium 410791
Show all pathways known for 1.8.1.14Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.14394071 Levels of acetyl coenzyme A, reduced and oxidized coenzyme A, and coenzyme A in disulfide linkage to protein in dormant germinated spores and growing and sporulating cells of Bacillus megaterium J. Bacteriol. 132 444-452 1979 Priestia megaterium QM 410791
Show all pathways known for 1.8.1.14Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.14712246 Michael acceptor-containing coenzyme A analogues as inhibitors of the atypical coenzyme A disulfide reductase from Staphylococcus aureus J. Am. Chem. Soc. 132 12853-12855 2010 Staphylococcus aureus 20738089
Show all pathways known for 1.8.1.14Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.14685514 N-Thiolated beta-lactams: Studies on the mode of action and identification of a primary cellular target in Staphylococcus aureus Bioorg. Med. Chem. 15 2453-2467 2007 Staphylococcus aureus 17258460
Results 1 - 10 of 23 > >>