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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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About This Item

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

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

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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.

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

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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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