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T7927

Sigma-Aldrich

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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25 UNITS
HUF 60,600.00
50 UNITS
HUF 175,000.00
250 UNITS
HUF 624,000.00

HUF 60,600.00

List PriceHUF 101,000.00Save 40%

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25 UNITS
HUF 60,600.00
50 UNITS
HUF 175,000.00
250 UNITS
HUF 624,000.00

About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

HUF 60,600.00

List PriceHUF 101,000.00Save 40%

Please contact Customer Service for Availability

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[1]
  • in a study to investigate the stereospecificity of sodium borohydride reduction of tyrosine decarboxylase[2]
  • in protein synthesis studies[3]

Biochem/physiol Actions

L-Tyrosine Decarboxylase Apoenzyme is an aromatic L-amino acid decarboxylase.[4] The enzyme activity of tyrosine decarboxylase (TDC) is dependent on the cofactor pyridoxal 5-phosphate (PLP).[5] It catalyzes the decarboxylation of dihydroxyphenylalanine.[4]

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.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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
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
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 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
Glenn E Bartley et al.
New biotechnology, 27(4), 308-316 (2010-04-21)
The phenolic amine synephrine is a vascoconstrictor and bronchiectatic agent and holds promise as an aid to weight management and obesity reduction. Synephrine is structurally similar to the active ingredients of several commercial cold remedies. Some Citrus contain high concentrations

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