T7927
L-Tyrosine Decarboxylase Apoenzyme from Streptococcus faecalis
<0.005 unit/mg solid (without pyridoxal 5-phosphate), ≥0.05 unit/mg solid (with excess pyridoxal 5-phosphate)
Synonym(s):
L-(−)-Tyrosine Apodecarboxylase, L-Tyrosine Carboxy-lase apoenzyme, TAD
Sign In to View Organizational & Contract Pricing.
Select a Size
About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-652-9
MDL number:
Specific activity:
≥0.05 unit/mg solid (with excess pyridoxal 5-phosphate), <0.005 unit/mg solid (without pyridoxal 5-phosphate)
Biological source:
Streptococcus faecalis
biological source
Streptococcus faecalis
form
powder
specific activity
≥0.05 unit/mg solid (with excess pyridoxal 5-phosphate), <0.005 unit/mg solid (without pyridoxal 5-phosphate)
storage temp.
−20°C
Quality Level
Application
L-Tyrosine decarboxylase apoenzyme from Streptococcus faecalis has been used:
- in a study to purify and characterize tyrosine decarboxylase and aromatic-L-amino-acid decarboxylase
- in a study to investigate the stereospecificity of sodium borohydride reduction of tyrosine decarboxylase
- in protein synthesis studies
Biochem/physiol Actions
L-Tyrosine Decarboxylase Apoenzyme is an aromatic L-amino acid decarboxylase. The enzyme activity of tyrosine decarboxylase (TDC) is dependent on the cofactor pyridoxal 5-phosphate (PLP). It catalyzes the decarboxylation of dihydroxyphenylalanine.
Other Notes
Dried cells grown on vitamin B6-deficient medium.
One unit will liberate 1.0 μmole of CO2 from L-tyrosine per min at pH 5.5 at 37 °C.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
新产品
This item has
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
J C Vederas et al.
The Journal of biological chemistry, 254(12), 5053-5057 (1979-06-25)
Sodium boro[3H]hydride reduction of tyrosine decarboxylase from Streptococcus faecalis followed by complete hydrolysis of the enzyme produces epsilon-[3H]pyridoxyllysine. Degradation of this material to [4'-3H]pyridoxamine and stereochemical analysis with apoaspartate aminotransferase shows that the re side at C-4' of the cofactor
T Miura et al.
International journal of cancer, 46(5), 931-934 (1990-11-15)
Phenolic melanin precursors can be utilized for the development of anti-melanoma agents. The sulphur homologue of tyrosine, 4-S-cysteinylphenol (CP) and its decarboxylation product, 4-S-cysteaminylphenol (CAP) were shown to be substrates of melanoma tyrosinase, forming melanin-like pigment. Both, but in particular
Haixia Zhu et al.
Scientific reports, 6, 27779-27779 (2016-06-14)
Tyrosine decarboxylase (TDC) is a pyridoxal 5-phosphate (PLP)-dependent enzyme and is mainly responsible for the synthesis of tyramine, an important biogenic amine. In this study, the crystal structures of the apo and holo forms of Lactobacillus brevis TDC (LbTDC) were
Gunsalus, I.C., and Smith, R.A.
Methods in Enzymology, 3, 963-963 (1957)
Estefanía Muñoz-Atienza et al.
International journal of food microbiology, 146(2), 212-216 (2011-03-18)
In this work, biogenic amine production (histamine, tyramine and putrescine) by a collection of 74 lactic acid bacteria of aquatic origin has been investigated by means of amino acid decarboxylation by growth on decarboxylase differential medium, biogenic amine detection by
Related Content
QC Methods
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service