Literature summary for 1.3.7.2 extracted from

Aras, M.; Hartmann, V.; Hartmann, J.; Nowaczyk, M.M.; Frankenberg-Dinkel, N.
Proximity channeling during cyanobacterial phycoerythrobilin synthesis (2020), FEBS J., 287, 284-294 .

Search for more literature for 1.3.7.2

Cloned(Commentary)

Cloned (Comment)	Organism
gene pebA, in Synechococcus sp. WH8020, the genes encoding for pebA and pebB share an overlapping region. The pebA stop codon TGA is part of the pebB start codon ATG, recombinant expression of a translational fusion between pebA and pebB, N-terminally Strep-tagged and C-terminally His-tagged PebAgB, recombinant expression of GST-tagged PebA in Escherichia coli BL21(DE3)	Synechococcus sp. WH 8020

Protein Variants

Protein Variants	Comment	Organism
additional information	analysis wether addition of PebB to the immobilized PebA-DHBV complex will result in the interaction of PebA and PebB and, therefore, cause retention of PebB on the column. Retention of PebB on the immobilized PebA column is not observed, but a transfer of almost all PebA-bound DHBV to PebB is seen, DHBV is washed off the column with regular washing buffer. in Synechococcus sp. WH8020, the genes encoding for pebA and pebB share an overlapping region. The pebA stop codon TGA is part of the pebB start codon ATG. In order to generate a translational fusion between pebA and pebB, a guanine base is inserted into the start-stop region of the pebAB-operon generating an artificial fusion of both enzymes, termed PebAgB. The newly generated codon GTG encodes for a valine residue, which then serves as a diminutive linker between PebA and PebB. This fusion protein is significantly different to the phage encoded PebS (EC 1.3.7.6), which is a homologue to PebA. But the fusion protein PebAgB shows PebS-like activity. Comparison of the PebAgB-catalyzed conversion of BV with an assay containing both PebA and PebB reveals no significant changes in velocity	Synechococcus sp. WH 8020

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	in cofactor ferredoxin	Synechococcus sp. WH 8020

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
biliverdin IXalpha + reduced ferredoxin	Synechococcus sp. WH 8020	-	15,16-dihydrobiliverdin + oxidized ferredoxin	-	?

Organism

Organism	UniProt	Comment	Textmining
Synechococcus sp. WH 8020	Q02189	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant GST-tagged PebA from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, gel filtration, and ultrafiltration, recombinant tagged PebAgB by affinity chromatography	Synechococcus sp. WH 8020

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
biliverdin IXalpha + reduced ferredoxin	-	Synechococcus sp. WH 8020	15,16-dihydrobiliverdin + oxidized ferredoxin	-	?

Synonyms

Synonyms	Comment	Organism
15,16-dihydrobiliverdin:ferredoxin oxidoreductase	-	Synechococcus sp. WH 8020
PebA	-	Synechococcus sp. WH 8020

Cofactor

Cofactor	Comment	Organism	Structure
Ferredoxin	-	Synechococcus sp. WH 8020

General Information

General Information	Comment	Organism
metabolism	during the biosynthesis of light-harvesting phycobilins in cyanobacteria, two members of the ferredoxin-dependent bilin reductases are involved in the reduction of the open-chain tetrapyrrole biliverdin IXa to the pink pigment phycoerythrobilin. The first reaction is catalyzed by 15,16-dihydrobiliverdin:ferredoxin oxidoreductase (PebA) and produces the unstable intermediate 15,16-dihydrobiliverdin (DHBV). This intermediate is subsequently channeled to and converted by phycoerythrobilin:ferredoxin oxidoreductase to the final product phycoerythrobilin. An on-column assay employing immobilized enzyme in combination with UV-Vis and fluorescence spectroscopy reveals that both enzymes transiently interact and that transfer of the intermediate is facilitated by a significantly higher binding affinity of DHBV toward phycoerythrobilin:ferredoxin oxidoreductase (PebB, EC 1.3.7.3). The intermediate DHBV is transferred via proximity channeling	Synechococcus sp. WH 8020

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Release 2023.1 (January 2023)