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B6db references: 85303115

type Journal Article
authors Buki, K. G.; Vinh, D. Q.; Horvath, I.
title Partial purification and some properties of tryptophan decarboxylase from a Bacillus strain
journal Acta Microbiol Hung
Activity 4.1.1.28
ui 85303115
year (1985)
volume 32
number 1
pages 65-73
 
keywords Aromatic-L-Amino-Acid Decarboxylases/antagonists & inhibitors/*isolation & purification/metabolism
abstract Bacteria of different origin were screened for tryptophan decarboxylase activity. The best producer belonged to an unidentified taxonomic entity of the genus Bacillus. In complete medium it produced tryptamine from tryptophan. The decarboxylase could partially be purified from the cells by sonication and DEAE-cellulose chromatography. The enzyme had an Mr of 150 000 and a pH optimum of about 7, was stable up to 37 degrees C, and its Km was about 0.3 mM for tryptophan. The enzyme needed pyridoxal phosphate for maximum activity.
last changed 2002/11/12 16:17

B6db references