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B6db references: 81069023

type Journal Article
authors Orlacchio, A.; Borri-Voltattorni, C.
title The steady state kinetics of tyrosine decarboxylase from Streptococcus faecalis
journal Ital J Biochem
ui 81069023
year (1979)
volume 28
number 1
pages 1-10.
keywords Enterococcus faecalis/*enzymology
abstract The present study has explained the general reaction mechanism of the bacterial tyrosine decarboxylase. The rate equation for this mechanism has been presented. The steady state kinetics of tyrosine decarboxylase, as for tyrosine transaminase, have shown that the apoenzyme can bind not only the coenzyme, but also the non- enzymatically formed Schiff base between the coenzyme and the substrate. Our data then have confirmed the importance of the non- enzymatically formed Schiff base in the B6-dependent enzymes, possibly in all of them which have a low affinity constant for the coenzyme, such that the coenzyme must be present in excess in respect to the protein to saturate the active center. The interaction between apotyrosine decarboxylase with pyridoxal-5'-phosphate and pyridoxamine- 5'-phosphate has been studied.
last changed 2002/11/12 16:17

B6db references