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Literature summary extracted from

  • Shang, L.; Rockwell, N.C.; Martin, S.S.; Lagarias, J.C.
    Biliverdin amides reveal roles for propionate side chains in bilin reductase recognition and in holophytochrome assembly and photoconversion (2010), Biochemistry, 49, 6070-6082.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.7.5 recombinant expression of GST-tagged PcyA in Escherichia coli Anabaena sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.7.5 biliverdin IXalpha + reduced ferredoxin Anabaena sp.
-
 phycocyanobilin + oxidized ferredoxin with biliverdins containing a single endovinyl group, such as BV IXalpha, PcyA can generate a mixture of 3E and 3Z products ?
1.3.7.5 biliverdin IXalpha + reduced ferredoxin Anabaena sp. PCC 7120
-
 phycocyanobilin + oxidized ferredoxin with biliverdins containing a single endovinyl group, such as BV IXalpha, PcyA can generate a mixture of 3E and 3Z products ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.7.5 Anabaena sp.
-
-
-
1.3.7.5 Anabaena sp. PCC 7120
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.7.5 recombinant GST-tagged PcyA from Escherichia coli by glutathione affinity chromatography Anabaena sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.7.5 biliverdin IXa diamide + reduced ferredoxin activity only at pH 6.0 Anabaena sp. ? + oxidized ferredoxin
-
 ?
1.3.7.5 biliverdin IXa diamide + reduced ferredoxin activity only at pH 6.0 Anabaena sp. PCC 7120 ? + oxidized ferredoxin
-
 ?
1.3.7.5 biliverdin IXalpha + reduced ferredoxin
-
 Anabaena sp. phycocyanobilin + oxidized ferredoxin with biliverdins containing a single endovinyl group, such as BV IXalpha, PcyA can generate a mixture of 3E and 3Z products ?
1.3.7.5 biliverdin IXalpha + reduced ferredoxin recombinant ferredoxin from Synechococcus sp. PCC7002 Anabaena sp. phycocyanobilin + oxidized ferredoxin with biliverdins containing a single endovinyl group, such as BV IXalpha, PcyA can generate a mixture of 3E and 3Z products ?
1.3.7.5 biliverdin IXalpha + reduced ferredoxin
-
 Anabaena sp. PCC 7120 phycocyanobilin + oxidized ferredoxin with biliverdins containing a single endovinyl group, such as BV IXalpha, PcyA can generate a mixture of 3E and 3Z products ?
1.3.7.5 biliverdin IXalpha + reduced ferredoxin recombinant ferredoxin from Synechococcus sp. PCC7002 Anabaena sp. PCC 7120 phycocyanobilin + oxidized ferredoxin with biliverdins containing a single endovinyl group, such as BV IXalpha, PcyA can generate a mixture of 3E and 3Z products ?
1.3.7.5 biliverdin IXalpha 12-monoamide + reduced ferredoxin
-
 Anabaena sp. phycocyanobilin 12-monoamide + oxidized ferredoxin products are corresponding phycocyanobilin monoamides with a mix of the 3E and 3Z forms ?
1.3.7.5 biliverdin IXalpha 12-monoamide + reduced ferredoxin
-
 Anabaena sp. PCC 7120 phycocyanobilin 12-monoamide + oxidized ferredoxin products are corresponding phycocyanobilin monoamides with a mix of the 3E and 3Z forms ?
1.3.7.5 biliverdin IXalpha 8-monoamide + reduced ferredoxin
-
 Anabaena sp. phycocyanobilin 8-monoamide + oxidized ferredoxin products are corresponding phycocyanobilin monoamides with a mix of the 3E and 3Z forms ?
1.3.7.5 biliverdin XIII + reduced ferredoxin
-
 Anabaena sp. phycocyanobilin + oxidized ferredoxin biliverdin XIII contains two endovinyl groups, so PcyA can convert either (or both) to an ethylidene ?
1.3.7.5 biliverdin XIIIalpha monoamide + reduced ferredoxin
-
 Anabaena sp. ? + oxidized ferredoxin mixture of products ?
1.3.7.5 additional information semisynthesis of mono- and diamides of biliverdin IXalpha, that function as substrates. The enzyme is accommodating to amidation of the propionic acid side chains of biliverdin IXalpha, which does not require free carboxylic acid side chains to yield its phytobilin product, phycocyanobilin. Bilin amides are assembled with BV-type apophytochromes, demonstrating a role for the 8-propionate in the formation of the spectroscopically native Pr dark states of the biliprotein photosensors. Neither ionizable propionate side chain proves to be essential to primary photoisomerization for BV-type phytochrome. No activity with biliverdin XIIIalpha diamide , but biliverdinXIII diacid is converted into the iso-PthetaB product with moderate yield Anabaena sp. ?
-
 ?
1.3.7.5 additional information semisynthesis of mono- and diamides of biliverdin IXalpha, that function as substrates. The enzyme is accommodating to amidation of the propionic acid side chains of biliverdin IXalpha, which does not require free carboxylic acid side chains to yield its phytobilin product, phycocyanobilin. Bilin amides are assembled with BV-type apophytochromes, demonstrating a role for the 8-propionate in the formation of the spectroscopically native Pr dark states of the biliprotein photosensors. Neither ionizable propionate side chain proves to be essential to primary photoisomerization for BV-type phytochrome. No activity with biliverdin XIIIalpha diamide , but biliverdinXIII diacid is converted into the iso-PthetaB product with moderate yield Anabaena sp. PCC 7120 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.3.7.5 PcyA
-
 Anabaena sp.
1.3.7.5 phycocyanobilin:ferredoxin oxidoreductase
-
 Anabaena sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.7.5 6
-
 assay with substrate biliverdin diamide Anabaena sp.
1.3.7.5 8.5
-
 assay at Anabaena sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.7.5 Ferredoxin dependent on Anabaena sp.

General Information

EC Number General Information Comment Organism
1.3.7.5 evolution comparison and discrimination of two bilin reductase families in bilin amide usage for photoconversions of BV-type and phytobilin-type phytochromes, mechanistic differences, overview Anabaena sp.
1.3.7.5 additional information the NADPH-dependent biliverdin reductases, BVR and BvdR, are less accommodating to amidation of the propionic acid side chains of biliverdin IXR than PcyA, which does not require free carboxylic acid side chains to yield its phytobilin product, phycocyanobilin Anabaena sp.