Abstract：
:A catechol oxidase from lemon balm (Melissa officinalis) moCO which only catalyzes the oxidation of catechols to quinones without hydroxylating tyrosine was purified. The molecular mass of the M. officinalis enzyme of 39,370 Da was obtained by MALDI mass spectrometry and the isoelectric point was determined to be 3.4. Addition of 2 eq. H(2)O(2) to the enzyme leads to oxy catechol oxidase. In the UV/Vis spectrum two new absorption bands occur at 343 nm (ε=8510 M(-1)cm(-1)) and 580 nm (ε=580 M(-1)cm(-1)) due to O(2)(2-)Cu (II) charge transfer transitions in accordance with the oxy forms of other type 3 copper proteins. The N-terminal sequence has been determined by Edman degradation to NPVQAPELDKCGTAT, exhibiting a proline at the second and sixth position conserved in other polyphenol oxidases.
journal_name
Phytochemistryjournal_title
Phytochemistryauthors
Rompel A,Büldt-Karentzopoulos K,Molitor C,Krebs Bdoi
10.1016/j.phytochem.2012.05.022subject
Has Abstractpub_date
2012-09-01 00:00:00pages
19-23eissn
0031-9422issn
1873-3700pii
S0031-9422(12)00243-9journal_volume
81pub_type
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