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

BRENDA support

Literature summary for 1.21.3.6 extracted from

  • Elumalai, P.; Liu, H.L.
    Homology modeling and dynamics study of aureusidin synthase--an important enzyme in aurone biosynthesis of snapdragon flower (2011), Int. J. Biol. Macromol., 49, 134-142.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
homology modeling using grenache polyphenol oxidase and sweet potato catechol oxidase as templates. The structure is folded into 15alpha-helices and 5 beta-sheets, and mostly composed by loops. The core of the enzyme is formed by a four-helix-bundle, and the helical bundle accommodates the dinuclear copper center. The cysteine residues Cys11, Cys25, Cys26, and Cys88 are highly conserved, and form disulfide bridges Antirrhinum majus

Inhibitors

Inhibitors Comment Organism Structure
Phenylthiourea modeling of enzyme-phenylthiourea complex. The inhibitor binds with the hydrophobic pocket of the dinuclear copper center. The phenyl ring of Phe262 and the imidazole ring of His245 form hydrophobic interactions with the aromatic ring of the inhibitor. The sulfur atom of the inhibitor replaces the hydroxo-bridge, which is essential for catalysis Antirrhinum majus

Metals/Ions

Metals/Ions Comment Organism Structure
copper two copper atoms, CuA and CuB, are located in the active site and each is coordinated by three histidine residues. CuA is coordinated by His87, His108, and His117 residues, while CuB is coordinated by His241, His245 and His275 Antirrhinum majus

Organism

Organism UniProt Comment Textmining
Antirrhinum majus Q9FRX6
-
-