Access

You are not currently logged in.

Access your personal account or get JSTOR access through your library or other institution:

login

Log in to your personal account or through your institution.

If You Use a Screen Reader

This content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.

Enzymology of L-Tyrosine Biosynthesis in Mung Bean (Vigna radiata [L.] Wilczek)

Judith L. Rubin and Roy A. Jensen
Plant Physiology
Vol. 64, No. 5 (Nov., 1979), pp. 727-734
Stable URL: http://www.jstor.org/stable/4265986
Page Count: 8
  • Read Online (Free)
  • Subscribe ($19.50)
  • Cite this Item
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Enzymology of L-Tyrosine Biosynthesis in Mung Bean (Vigna radiata [L.] Wilczek)
Preview not available

Abstract

The enzymes of the 4-hydroxyphenylpyruvate (prephenate dehydrogenase and 4-hydroxyphenylpyruvate aminotransferase) and pretyrosine (prephenate aminotransferase and pretyrosine dehydrogenase) pathways of L-tyrosine biosynthesis were partially purified from mung bean (Vigna radiata [L.] Wilczek) seedlings. NADP-dependent prephenate dehydrogenase and pretyrosine dehydrogenase activities coeluted from ion exchange, adsorption, and gel-filtration columns, suggesting that a single protein (52,000 daltons) catalyzes both reactions. The ratio of the activities of partially purified prephenate to pretyrosine dehydrogenase was constant during all purification steps as well as after partial inactivation caused by p-hydroxymercuribenzoic acid or heat. The activity of prephenate dehydrogenase, but not of pretyrosine dehydrogenase, was inhibited by L-tyrosine at nonsaturating levels of substrate. The $\text{K}_{m}$ values for prephenate and pretyrosine were similar, but the specific activity with prephenate was 2.9 times greater than with pretyrosine. Two peaks of aromatic aminotransferase activity utilizing L-glutamate or L-aspartate as amino donors and 4-hydroxyphenylpyruvate, phenylpyruvate, and/or prephenate as keto acid substrates were eluted from DEAE-cellulose. Of the three keto acid substrates, 4-hydroxyphenylpyruvate was preferentially utilized by 4-hydroxyphenylpyruvate aminotransferase whereas prephenate was best utilized by prephenate aminotransferase. The identity of a product of prephenate aminotransferase as pretyrosine following reaction with prephenate was established by thin layer chromatography of the dansyl-derivative.

Page Thumbnails

  • Thumbnail: Page 
727
    727
  • Thumbnail: Page 
728
    728
  • Thumbnail: Page 
729
    729
  • Thumbnail: Page 
730
    730
  • Thumbnail: Page 
731
    731
  • Thumbnail: Page 
732
    732
  • Thumbnail: Page 
733
    733
  • Thumbnail: Page 
734
    734