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Literature summary extracted from

  • Wada, K.; Hagiwara, Y.; Yutani, Y.; Fukuyama, K.
    One residue substitution in PcyA leads to unexpected changes in tetrapyrrole substrate binding (2010), Biochem. Biophys. Res. Commun., 402, 373-377.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.7.5 purified recombinant enzyme mutant V225D in complex with substrates biliverdin IXalpha or biliverdin XIIIalpha, mixing of 0.0009 ml of protein solution, containing 11.5 mg/ml protein and biliverdin, with 0.0009 ml of reservoir solution containing 0.8-1.0 M NaH2PO4, 1.0-1.2 M K2HPO4, and 100 mM sodium acetate, pH 4.0, 20°C, a few days, X-ray diffraction structure determination and analysis at 1.9 A resolution Synechocystis sp.

Protein Variants

EC Number Protein Variants Comment Organism
1.3.7.5 V225D site-directed mutagenesis,substrate binding structure, overview 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 XIIIalpha + reduced ferredoxin
-
Synechocystis sp. ? + oxidized ferredoxin
-
?

Synonyms

EC Number Synonyms Comment Organism
1.3.7.5 PcyA
-
Synechocystis sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.7.5 Ferredoxin
-
Synechocystis sp.