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T7927

Sigma-Aldrich

L-Tyrosin-Decarboxylase-Apoenzym aus Streptococcus faecalis

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

Synonym(e):

L-(−)-Tyrosin-Apodecarboxylase, TAD

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About This Item

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

Biologische Quelle

Streptococcus faecalis

Form

powder

Spezifische Aktivität

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

Lagertemp.

−20°C

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Anwendung

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. Wirkung

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.

Sonstige Hinweise

Dried cells grown on vitamin B6-deficient medium.

Einheitendefinition

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

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)

Analysenzertifikate (COA)

Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.

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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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