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B6db references: 24310513

type Journal Article
authors No W, Mollenschott C, Berlin J.
title Tryptophan decarboxylase from Catharanthus roseus cell suspension cultures: purification, molecular and kinetic data of the homogenous protein
journal Plant Mol Biol
sel unselected
ui 24310513
year (1984)
volume 3
number 5
pages 281-8
keywords DOI: 10.1007/BF00017782
abstract The purification of tryptophan decarboxylase from Catharanthus roseus (TDC, E.C.:, to apparent homogeneity, is described. The enzyme represents a soluble protein with a molecular weight of 115 0003 000, consisting of 2 identical subunits of 54 0001 000. The pI was estimated to be 5.9 and the Km for L-tryptophan was found to be 7.510(-5) M. Phenylalanine, tyrosine and DOPA were not decarboxylated by tryptophan decarboxylase from Catharanthus cells. Similar to the aromatic amino acid decarboxylase from hog kidney the enzyme does not appear to be obligatorily dependent on exogenously supplied pyridoxal phosphate, as it seems to contain a certain amount of this cofactor. The average percentage of TDC in the cells was found to be 0.002% in the growth medium while the level increased up to 0.03% when indole alkaloid biosynthesis was induced. The role of the protein as a bottleneck enzyme of indole alkaloid biosynthesis is discussed.
last changed 2018/05/17 13:01

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