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Literature summary for 1.3.7.5 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)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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

Synonyms Comment Organism
PcyA
-
Synechocystis sp.

Cofactor

Cofactor Comment Organism Structure
Ferredoxin
-
Synechocystis sp.

General Information

General Information Comment Organism
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.
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.