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Literature summary for 1.3.7.5 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
Search for more literature for 1.3.7.5

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
V225D site-directed mutagenesis,substrate binding structure, overview Synechocystis sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
biliverdin Ixalpha + reduced ferredoxin Synechocystis sp.
-
 (3Z)-phycocyanobilin + oxidized ferredoxin
-
 ?

Organism

Organism UniProt Comment Textmining
Synechocystis sp. Q55891
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
biliverdin Ixalpha + reduced ferredoxin
-
 Synechocystis sp. (3Z)-phycocyanobilin + oxidized ferredoxin
-
 ?
biliverdin XIIIalpha + reduced ferredoxin
-
 Synechocystis sp. ? + oxidized ferredoxin
-
 ?

Synonyms

Synonyms Comment Organism
PcyA
-
 Synechocystis sp.

Cofactor

Cofactor Comment Organism Structure
Ferredoxin
-
 Synechocystis sp.