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
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About This Item
biological source
Streptococcus faecalis
Quality Level
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
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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.
Unit Definition
One unit will liberate 1.0 μmole of CO2 from L-tyrosine per min at pH 5.5 at 37 °C.
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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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
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
T Komprda et al.
Meat science, 86(3), 870-877 (2010-08-11)
Lactic acid bacteria (LAB) and enterococci were isolated immediately after stuffing (day 0), at the end of ripening (28th day) and at the end of storage (112th day) from dry fermented sausages produced by two different producers (K; R) in
Purification and characterisation of tyrosine decarboxylase and aromatic-L-amino-acid decarboxylase.
T Børresen et al.
Biochimica et biophysica acta, 993(1), 108-115 (1989-10-13)
Microbial tyrosine decarboxylase (EC 4.1.1.25) and mammalian aromatic-L-amino-acid decarboxylase (EC 4.1.1.28) catalyse the formation of tyramine from L-tyrosine. These enzymes were characterised after isolation to purity by methods including fast polymer liquid chromatography (FPLC). Tyrosine decarboxylase was isolated from Streptococcus
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