Journal ArticleDOI
An abnormal reaction occurring in the presence of L-aromatic aminoacid decarboxylase.
E. Barboni,C. Borri Voltattorni,Maria D'Erme,A. Fiori,Alba Minelli,Maria Anna Rosei,Carlo Turano +6 more
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TLDR
Evidence is presented which rules out the possibility that this phenomenon is due to an oxidative deamination, and the reaction cannot be simply a decarboxylation-dependent transamination, using the coenzyme as an amino group acceptor.About:
This article is published in Biochemical and Biophysical Research Communications.The article was published on 1981-03-31. It has received 17 citations till now. The article focuses on the topics: Oxidative deamination & Transamination.read more
Citations
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Journal ArticleDOI
Transaminations catalysed by brain glutamate decarboxylase.
TL;DR: The transamination was reversible, and apoenzyme could be reconstituted to holoenzyme by reverse transamination with succinic semialdehyde and pyridoxamine 5'-phosphate, suggesting that the decarboxylation step is not entirely rate-limiting in the normal mechanism.
Journal ArticleDOI
Reaction Specificity of Native and Nicked 3,4-Dihydroxyphenylalanine Decarboxylase *
TL;DR: It is suggested that native Dopa decarboxylase can exist as an equilibrium among “open,” “half-open” and “closed” forms.
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Inactivation of brain glutamate decarboxylase and the effects of adenosine 5'-triphosphate and inorganic phosphate.
Mary P. Meeley,David L. Martin +1 more
TL;DR: Glutamate-promoted inactivation, its enhancement by ATP, and the opposition to inactivation by pyridoxal-P and Pi appear to be important in the regulation of glutamate decarboxylase.
Journal ArticleDOI
Interaction of aromatic amino acids in D- and L-forms with 3,4-dihydroxyphenylalanine decarboxylase from pig kidney
Journal ArticleDOI
Mechanism-based Inactivation of Dopa Decarboxylase by Serotonin
TL;DR: Findings indicate that 5-HT is both a substrate and a mechanism-based inactivator with a partition ratio for product formation versus inactivation of 21.5:1, and that protection from inactivation by 5- HT was observed in the presence of the active site-directed inhibitor 3,4-dihydroxy-D-phenylalanine.
References
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Journal ArticleDOI
Measurement of low energy beta-emitters in aqueous solution by liquid scintillation counting of emulsions.
M. S. Patterson,R. C. Greene +1 more
Journal ArticleDOI
The enzymatic oxidation of pyridoxine and pyridoxamine phosphates.
Hiroshi Wada,Esmond E. Snell +1 more
TL;DR: In the course of these investigations, a simple photometric method has been developed for the determination of pyridoxal or pyrIDoxal S-phosphate in enzymatic reaction mixtures and it is concluded that the two enzymes are probably identical.
Journal ArticleDOI
Preparation and properties of a homogeneous aromatic l-amino acid decarboxylase from hog kidney
TL;DR: Preparations of hog kidney aromatic l -amino acid decarboxylase have been obtained which are 99% pure as indicated by disc gel electrophoresis, sedimentation, and immunological techniques, and added pyridoxal phosphate stimulated the activity up to fivefold.
Journal ArticleDOI
Purification and Characterization of 3,4-Dihydroxyphenylalanine Decarboxylase from Pig Kidney
TL;DR: A procedure for 3,4-dihydroxyphenylalanine decarboxylase from pig kidney purification is described in detail and results are consistent with the existence of at least four coenzyme-apoenzyme complexes, three of them active.
Related Papers (5)
Decarboxylation-dependent transamination catalyzed by mammalian 3,4-dihydroxyphenylalanine decarboxylase.
M H O'Leary,R L Baughn +1 more