Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Kohler, A.C.; Gae, D.D.; Richley, M.A.; Stoll, S.; Gunn, A.; Lim, S.; Martin, S.S.; Doukov, T.I.; Britt, R.D.; Ames, J.B.; Lagarias, J.C.; Fisher, A.J.
    Structural basis for hydration dynamics in radical stabilization of bilin reductase mutants (2010), Biochemistry, 49, 6206-6218.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.7.5 expression of mutant enzymes in Escherichia coli strain BL21(DE3) Synechocystis sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.7.5 purified recombinant mutant enzymes, hanging drop vapour diffusion method, dithionite-treated reduced D105N PcyA crystals from 1.45-1.8 M ammonium sulfate, 0.15-0.4 M NaCl, and 0.1 M HEPES, pH 7.0, dithionite-treated reduced H88Q PcyA crystals from 1.7-2.2 M ammonium sulfate, 0.26-0.32 M NaCl, and 0.1 M sodium cacodylate, pH 7.0, 20°C in the dark, cryoprotectant solution is consisting of 30% v/v ethylene glycol in mother liquor, X-ray diffraction structure determination and analysis at 1.5 A resolution Synechocystis sp.

Protein Variants

EC Number Protein Variants Comment Organism
1.3.7.5 D105N site-directed mutagenesis Synechocystis sp.
1.3.7.5 H88Q site-directed mutagenesis 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.
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.7.5 recombinant mutant enzymes from Escherichia coli strain BL21(DE3) by cyanide affinity chromatography Synechocystis sp.

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
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.7.5 More both PcyA D105N and H88Q mutants adopt alpha/beta/alpha sandwich folds possessing a central seven-stranded antiparallel beta-sheet lying between four alpha-helixes on each side Synechocystis sp.

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.

General Information

EC Number General Information Comment Organism
1.3.7.5 metabolism phycocyanobilin:ferredoxin oxidoreductase, PcyA, is a key enzyme in the biogenesis of heme-derived linear tetrapyrroles, phytobilins, it catalyzes the overall four-electron reduction of biliverdin IXalpha to phycocyanobilin, the common chromophore precursor for both classes of biliproteins Synechocystis sp.
1.3.7.5 additional information the interconversion occurs via semireduced bilin radical intermediates that are profoundly stabilized by selected mutations of two critical catalytic residues, Asp105 and His88. Mechanistic scheme for PcyA-mediated reduction of both vinyl groups of biliverdin wherein an axial water molecule, which prematurely binds and ejects from both mutants upon one electron reduction, is required for catalytic turnover of the semireduced state, structure-function relationship, overview Synechocystis sp.