Refine search

Search Application

Search term:

Results 1 - 2 of 2

download as CSV

download all results as CSV

EC Number	Application	Commentary	Reference
4.4.1.32	synthesis	production of of a fluorescent holo-C-phycocyanin subunit alpha in Escherichia coli by construction of an expression vector containing five essential genes in charge of biosynthesis of cyanobacterial C-phycocyanin holo-alpha subunit. The vector harbors two cassettes: one cassette carries genes hox1 and pcyA required for conversion of heme to phycocyanobilin, and the other cassette carries cpcA encoding C-phycocyanin subunit alpha along with lyase subunits cpcE and cpcF both of which are necessary and sufficient for the correct addition of phycobiliprotein to CpcA. The maximum peak of absorbance spectrum is at 623 nm, and the maximum peak of fluorescence emission and excitation are at 648 and 633 nm, respectively, which are similar to those of native C-phycocyanin	731155
4.4.1.32	synthesis	reconstitution of the entire pathway for the synthesis of a fluorescent holophycobiliprotein subunit from Synechocystis sp. PCC6803 in Escherichia coli. Heme oxygenase 1 and 3Z-phycocyanobilin:ferredoxin oxidoreductase are expressed from one plasmid. Genes for the apoprotein C-phycocyanin a subunit, cpcA and the heterodimeric lyase subunit cpcE and cpcF that catalyze chromophore attachment are expressed from a second plasmid. Upon induction, recombinant Escherichia coli uses the cellular pool of heme to produce holo-CpcA with spectroscopic properties qualitatively and quantitatively similar to those of the same protein produced endogenously in cyanobacteria. About a third of the apo-CpcA is converted to holo-CpcA	437764

Results 1 - 2 of 2

download as CSV

download all results as CSV

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)