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Results 1 - 10 of 22 > >>
EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.29748716 Molecular cloning of CpcU and heterodimeric bilin lyase activity analysis of CpcU and CpcS for attachment of phycocyanobilin to Cys-82 on the beta-subunit of phycocyanin in Arthrospira platensis FACHB314 Molecules 21 357 2016 Arthrospira platensis 26999083
Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.29748716 Molecular cloning of CpcU and heterodimeric bilin lyase activity analysis of CpcU and CpcS for attachment of phycocyanobilin to Cys-82 on the beta-subunit of phycocyanin in Arthrospira platensis FACHB314 Molecules 21 357 2016 Arthrospira platensis FACHB314 26999083
Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.29732032 Biogenesis of phycobiliproteins: I. cpcS-I and cpcU mutants of the cyanobacterium Synechococcus sp. PCC 7002 define a heterodimeric phyococyanobilin lyase specific for beta-phycocyanin and allophycocyanin subunits J. Biol. Chem. 283 7503-7512 2008 Synechococcus sp. 18199754
Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.29732033 Biogenesis of phycobiliproteins: II. CpcS-I and CpcU comprise the heterodimeric bilin lyase that attaches phycocyanobilin to CYS-82 OF beta-phycocyanin and CYS-81 of allophycocyanin subunits in Synechococcus sp. PCC 7002 J. Biol. Chem. 283 7513-7522 2008 Synechococcus sp. 18199753
Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.29732033 Biogenesis of phycobiliproteins: II. CpcS-I and CpcU comprise the heterodimeric bilin lyase that attaches phycocyanobilin to CYS-82 OF beta-phycocyanin and CYS-81 of allophycocyanin subunits in Synechococcus sp. PCC 7002 J. Biol. Chem. 283 7513-7522 2008 Synechococcus sp. ATCC 27264 18199753
Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.29731173 Biosynthesis of cyanobacterial phycobiliproteins in Escherichia coli: Chromophorylation efficiency and specificity of all bilin lyases from Synechococcus sp. strain PCC 7002 Appl. Environ. Microbiol. 76 2729-2739 2010 Synechococcus sp. 20228104
Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.29732034 Catalytic mechanism of S-type phycobiliprotein lyase: chaperone-like action and functional amino acid residues J. Biol. Chem. 284 36405-36414 2009 Anabaena sp. 19864423
Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.29732034 Catalytic mechanism of S-type phycobiliprotein lyase: chaperone-like action and functional amino acid residues J. Biol. Chem. 284 36405-36414 2009 Anabaena sp. PCC 7120 19864423
Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.29732040 Characterization of the activities of the CpeY, CpeZ, and CpeS bilin lyases in phycoerythrin biosynthesis in Fremyella diplosiphon strain UTEX 481 J. Biol. Chem. 286 35509-35521 2011 Microchaete diplosiphon 21865169
Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.29674771 Chromophore attachment to phycobiliprotein beta-subunits: phycocyanobilin:cysteine-beta84 phycobiliprotein lyase activity of CpeS-like protein from Anabaena Sp. PCC7120 J. Biol. Chem. 281 8573-8581 2006 Anabaena sp. 16452471
Results 1 - 10 of 22 > >>