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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)

Sinonimo/i:

L-(−)-Tyrosine Apodecarboxylase, L-Tyrosine Carboxy-lase apoenzyme, TAD

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About This Item

Numero CAS:
9002-09-9
Classificazione EC (Enzyme Commission):
4.1.1.25 (BRENDA, IUBMB)
Numero CE:
232-652-9
Numero MDL:
MFCD00131472
Codice UNSPSC:
12352204
NACRES:
NA.54

Origine biologica

Streptococcus faecalis

Livello qualitativo

200

Stato

powder

Attività specifica

≥0.05 unit/mg solid (with excess pyridoxal 5-phosphate)
<0.005 unit/mg solid (without pyridoxal 5-phosphate)

Temperatura di conservazione

−20°C

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Applicazioni

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

Azioni biochim/fisiol

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.

Altre note

Dried cells grown on vitamin B6-deficient medium.

Definizione di unità

One unit will liberate 1.0 μmole of CO2 from L-tyrosine per min at pH 5.5 at 37 °C.

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)

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Certificati d'analisi (COA)

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

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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
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
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
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