Crystallization and preliminary X‐ray crystallographic analysis of polyphenol oxidase from Juglans regia (jrPPO1). Issue 6 (1st June 2014)

• Record Type: Journal Article
• Authors: Zekiri, Florime; Bijelic, Aleksandar; Molitor, Christian; Rompel, Annette
• Is Part Of: Acta crystallographica. Volume 70:Issue 6(2014:Jun.)
• Page Start: 832
• Page End: 834
• Publication Date: 2014-06-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X1400884X
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Tyrosinase is a type 3 copper enzyme that catalyzes the <italic>ortho</italic>‐hydroxylation of monophenols to diphenols as well as their subsequent oxidation to quinones, which are precursors for the biosynthesis of melanins. The first plant tyrosinase from walnut leaves (<italic>Juglans regia</italic>) was purified to homogeneity and crystallized. During the purification, two forms of the enzyme differing only in their C‐termini [<italic>jr</italic>PPO1(Asp¹⁰¹–Pro⁴⁴⁴) and <italic>jrPPO1</italic>(Asp¹⁰¹–Arg⁴⁴⁵)] were obtained. The most abundant form <italic>jr</italic>PPO1(Asp¹⁰¹–Arg⁴⁴⁵), as described in Zekiri <italic>et al.</italic> [<italic>Phytochemistry</italic> (2014), <bold>101</bold>, 5–15], was crystallized, resulting in crystals that belonged to space group <italic>C</italic>121, with unit‐cell parameters <italic>a</italic> = 115.56, <italic>b</italic> = 91.90, <italic>c</italic> = 86.87 Å, α = 90, β = 130.186, γ = 90°, and diffracted to 2.39 Å resolution. Crystals were only obtained from solutions containing at least 30% polyethylene glycol 5000 monomethyl ether in a close‐to‐neutral pH range.</p> </abstract>