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Results 1 - 10 of 81 > >>
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EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Show all pathways known for 1.1.1.36Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.36761574 An NADH preferring acetoacetyl-CoA reductase is engaged in poly-3-hydroxybutyrate accumulation in Escherichia coli J. Biotechnol. 325 207-216 2021 Candidatus Accumulibacter phosphatis 33122026
Show all pathways known for 1.1.1.36Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.36761574 An NADH preferring acetoacetyl-CoA reductase is engaged in poly-3-hydroxybutyrate accumulation in Escherichia coli J. Biotechnol. 325 207-216 2021 Candidatus Accumulibacter phosphatis UW-1 33122026
Show all pathways known for 1.1.1.36Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.36760524 Binding of NADP+ triggers an open-to-closed transition in a mycobacterial FabG beta-ketoacyl-ACP reductase Biochem. J. 474 907-921 2017 Mycolicibacterium smegmatis 28126742
Show all pathways known for 1.1.1.36Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.36760524 Binding of NADP+ triggers an open-to-closed transition in a mycobacterial FabG beta-ketoacyl-ACP reductase Biochem. J. 474 907-921 2017 Mycolicibacterium smegmatis mc2155 28126742
Show all pathways known for 1.1.1.36Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.36761573 Characterization of polyhydroxyalkanoate synthases from the marine bacterium Neptunomonas concharum JCM17730 J. Biotechnol. 319 69-73 2020 Neptunomonas concharum 32526261
Show all pathways known for 1.1.1.36Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.36761573 Characterization of polyhydroxyalkanoate synthases from the marine bacterium Neptunomonas concharum JCM17730 J. Biotechnol. 319 69-73 2020 Neptunomonas concharum JCM17730 32526261
Show all pathways known for 1.1.1.36Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.36760305 Crystal structure of acetoacetyl-CoA reductase from Rickettsia felis Acta Crystallogr. Sect. F 77 54-60 2021 Rickettsia felis 33620038
Show all pathways known for 1.1.1.36Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.36760305 Crystal structure of acetoacetyl-CoA reductase from Rickettsia felis Acta Crystallogr. Sect. F 77 54-60 2021 Rickettsia felis ATCC VR-1525 33620038
Show all pathways known for 1.1.1.36Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.36761545 Molecular mechanism of acetoacetyl-CoA enhanced kinetics for increased bioplastic production from Cupriavidus necator 428 J. Biomol. Struct. Dyn. 38 827-840 2020 Cupriavidus necator 30836854
Show all pathways known for 1.1.1.36Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.36761545 Molecular mechanism of acetoacetyl-CoA enhanced kinetics for increased bioplastic production from Cupriavidus necator 428 J. Biomol. Struct. Dyn. 38 827-840 2020 Cupriavidus necator DSM 428 30836854
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