Accession Number:

AD0631263

Title:

AROMATIC METABOLISM IN PLANTS. I. A STUDY OF THE PREPHENATE DEHYDROGENASE FROM BEAN PLANTS,

Descriptive Note:

Corporate Author:

PRAIRIE REGIONAL LAB SASKATOON (SASKATCHEWAN)

Personal Author(s):

Report Date:

1965-06-14

Pagination or Media Count:

8.0

Abstract:

Prephenate dehydrogenase prephenate NADP oxidoreductase decarboxylating was isolated from cotyledons of wax bean Phaseolus vulgaris L. var. Bountiful. The enzyme utilizes NADP as an oxidant. The optimum pH for activity is 7.5, and the maximum stability of the enzyme at 22 degrees is achieved in the pH range from 7 to 8. The enzyme is inhibited by sulphydryl complexing compounds. Addition of phenylalanine, tyrosine, or cinnamate did not depress the rate of formation of 4-hydroxyphenylpyruvate. The prephenate dehydrogenase also is present in the cotyledons and the shoots of mung bean Phaseolus aureus Roxb.. A study was made of the variation in the amount of prephenate dehydrogenase and aromatic amino acid transaminase in developing mung bean plants. The results show that the dehydrogenase is present in largest concentration in the cotyledons 4-5 days after germination has been initiated, and the transaminase reaches the highest level in the shoots after 12-14 days of growth. Author

Subject Categories:

  • Biochemistry

Distribution Statement:

APPROVED FOR PUBLIC RELEASE