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Literature summary extracted from

  • Hagiwara, Y.; Sugishima, M.; Khawn, H.; Kinoshita, H.; Inomata, K.; Shang, L.; Lagarias, J.C.; Takahashi, Y.; Fukuyama, K.
    Structural insights into vinyl reduction regiospecificity of phycocyanobilin:ferredoxin oxidoreductase (PcyA) (2010), J. Biol. Chem., 285, 1000-1007.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.7.5 purified recombinant wild-type PcyA and PcyA-E76Q mutant in complex with 18EtBV or biloverdin IXalpha and biliverdin XIIIalpha, hanging drop vapor diffusion method, 20°C, method optimization, protein solution containing wild-type PcyA or mutant E76Q and bilin is mixed with reservoir solutions containing 0.85 M sodium citrate, 0.1 M sodium cacodylate, pH 7.0, for the PcyA-18EtBV complex and 2.0 M ammonium sulfate, 0.2 M NaCl, and 0.1M sodium cacodylate, pH7.0, for the PcyA-BV13 complex, for the mutant a reservoir solution containing 1.7 M ammonium sulfate, 2% PEG 400, and 0.1 M HEPES, pH 7.0, is used, X-ray diffraction structure determination and analysis at 1.04-1.48 A resolution Synechocystis sp.

Protein Variants

EC Number Protein Variants Comment Organism
1.3.7.5 E76Q site-directed mutagenesis, substrate-binding structure compared to the wild-type enzyme. Overall folds and the binding sites of the U-shaped substrates of all three complexes are similar with wild-type PcyABV, the orientation of the Glu76 side chain, which is in close contact with the exo-vinyl group in PcyA-biliverdin IXalpha, is rotated away from the bilin D-ring. The local structures around the A-rings in the three complexes, which all retain the ability to reduce the A-ring of their bound pigments, are nearly identical with that of wild-type PcyA-biliverdin IXalpha Synechocystis 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 Synechocystis sp.
-
 (3Z)-phycocyanobilin + oxidized ferredoxin
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.7.5 Synechocystis sp. Q55891
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.7.5 biliverdin Ixalpha + reduced ferredoxin
-
 Synechocystis sp. (3Z)-phycocyanobilin + oxidized ferredoxin
-
 ?
1.3.7.5 biliverdin Ixalpha + reduced ferredoxin proton-donating role of the carboxylic acid side chain of residue Glu76 for exo-vinyl reduction, structural basis for the reduction regiospecificity of PcyA, overview Synechocystis sp. (3Z)-phycocyanobilin + oxidized ferredoxin
-
 ?
1.3.7.5 biliverdin XIIIalpha + reduced ferredoxin a synthetic substrate that lacks an exo-vinyl group Synechocystis sp. ? + oxidized ferredoxin
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.3.7.5 PcyA a member of the ferredoxin-dependent bilin reductase family Synechocystis sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.7.5 8.5
-
 assay at Synechocystis sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.7.5 Ferredoxin recombinantly expressed in Escherichia coli strains C41(DE3) Synechocystis sp.

General Information

EC Number General Information Comment Organism
1.3.7.5 physiological function unlike other ferredoxin-dependent bilin reductases that catalyze a two-electron reduction, PcyA sequentially reduces D-ring (exo) and A-ring (endo) vinyl groups of biliverdin IXalpha to yield phycocyanobilin, a key pigment precursor of the light-harvesting antennae complexes of red algae, cyanobacteria, and cryptophytes Synechocystis sp.