anchusa littorea/tyrosine

Three activities of tyrosine aminotransferase (TAT; EC 2.6.1.5), the enzyme which catalyzes the first step of the tyrosine pathway leading to the formation of rosmarinic acid (alpha-O-caffeoyl-3,4-dihydroxyphenyllactic acid), have been extensively purified from cell suspension cultures of Anchusa

Time-course changes in rosmarinic acid (RA) formation and activities of tyrosine aminotransferase (TAT) isoforms were examined in Anchusa officinalis suspension cultures. Three TAT isoforms (TAT-1, TAT-3, TAT-4) were resolved by Mono-Q anion-exchange column chromatography. The proportion of the

Prephenate aminotransferase (PAT) from rosmarinic acid-producing cell cultures of Anchusa officinalis has been purified to apparent electrophoretic homogeneity using a combination of high-performance anion-exchange, chromatofocusing, and gel filtration chromatography. The purified enzyme has a

The pool sizes of free l-phenylalanine and l-tyrosine, the precursors of rosmarinic acid in Anchusa officinalis L. cell suspension cultures, fluctuated during the culture cycle. The major increase in pool sizes was preceded by a peak of prephenate aminotransferase activity, while the subsequent

Cancer is one of the chronic health conditions worldwide. Various therapeutically active compounds from medicinal plants were the current focus of this research in order to uncover a treatment regimen for cancer. Anchusa arvensis (A. anchusa) (L.) M.Bieb.