Journal Article

Enzymatic Conversion of Pheophorbide <i>a</i> to the Precursor of Pyropheophorbide <i>a</i> in Leaves of <i>Chenopodium album</i>

Yuzo Shioi, Kenji Watanabe and Ken-ichiro Takamiya

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 37, issue 8, pages 1143-1149
Published in print December 1996 | ISSN: 0032-0781
e-ISSN: 1471-9053 | DOI:
Enzymatic Conversion of Pheophorbide a to the Precursor of Pyropheophorbide a in Leaves of Chenopodium album

More Like This

Show all results sharing these subjects:

  • Biochemistry
  • Molecular and Cell Biology
  • Plant Sciences and Forestry


Show Summary Details


Soluble proteins extracted from leaves of Chenopodium album catalyzed the conversion of pheophorbide a to a precursor of pyropheophorbide a, putatively identified as C-132-carboxyl-pyropheophorbide a. The precursor was then decarboxylated non-enzymatically to yield pyropheophorbide a. Soluble proteins and pheophorbide a, as the substrate, were required for the formation of the precursor, and boiled proteins were enzymatically inactive. The maximum rate of conversion of pheophorbide a to the precursor occurred at pH 7.5. The Km for pheophorbide a was 12.5 μM at pH 7.0. Both pheophorbide b and bacteriopheophorbide a could serve as substrates, but protopheophorbide a could not. Formation of methanol was detected during the enzymatic reaction, an indication that the enzyme is an esterase. Among seven alcohol analogs tested, only methanol inhibited the enzymatic activity uncompetitively, with a K1 of 71.6 mM. Mass-spectrometric (MS) analysis of the precursor yield a peak at m/z 579 that indicated the release of a methyl group from pheophorbide a. It appears therefore that the enzyme catalyzes the demethylation of the carbomethoxy group at C-132 of pheophorbide a by hydrolysis to yield methanol and the precursor, C-132-carboxyl-pyropheophorbide a, which is converted to pyropheophorbide a by spontaneous decarboxylation. We have tentatively designated the enzyme “pheophorbidase”. The presence of the enzyme was dependent on plant species and it was expressed constitutively.

Keywords: Chenopodium album; Chlorophyll breakdown; Pheophorbidase; Pyropheophorbide formation

Journal Article.  0 words. 

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

Full text: subscription required

How to subscribe Recommend to my Librarian

Users without a subscription are not able to see the full content. Please, subscribe or login to access all content.