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Merck
CN

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

CAS Number:
9002-09-9
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-652-9
MDL number:
MFCD00131472
EC Number:
4.1.1.25 (BRENDA, IUBMB)
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

Key Documents

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Product Name

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)

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

200

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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.
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

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Certificates of Analysis (COA)

Lot/Batch Number
121H00682
121H00681
091H06381
091H06382

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Gunsalus, I.C., and Smith, R.A.
Methods in Enzymology, 3, 963-963 (1957)
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
E E Smissman et al.
Journal of medicinal chemistry, 19(1), 161-163 (1976-01-01)
2,2-Dimethyl-4-imidazolidinone derivatives of the alpha-amino acids DL-phenylglycine (1), DL-phenylalanine (2), L-tyrosine (3), L-histidine (4), and L-tryptophan (5) were prepared in order to assess their specificity in inhibiting amino acid decarboxylases. Treatment of th alpha-aminonitriles with acetone in the presence of
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