| Identification | Back Directory | [Name]
EC 4.1.1.25 | [CAS]
9002-09-9 | [Synonyms]
EC 4.1.1.25
EC 4.1.1.25 USP/EP/BP
Decarboxylase, tyrosine
L-TYROSINE CARBOXY-LYASE
L-TYROSINE DECARBOXYLASE
fromstreptococcusfaecalis
l-(-)-tyrosine apodecarboxylase
L-Tyrosine Carboxy-lase apoenzyme
L-TYROSINE DECARBOXYLASE APOENZYME
L-TYROSINE DECARBOXYLASE FROM STREPTO- &
L-Tyrosine Decarboxylase Streptococcus faecalis
L-tyrosine decarboxylase from strepto-coccus faecalis
Tyrosine Decarboxylase froM Streptococcus faecalis(NCTC6783)
l-tyrosine decarboxylase apoenzyme from streptococcus faecalis
Tyrosine Decarboxylase from Streptococcus faecalis(NCTC6783)(Apoenzyme)
L-(-)-Tyrosine Apodecarboxylase, L-Tyrosine Carboxy-lase apoenzyme, TAD | [EINECS(EC#)]
232-652-9 | [MDL Number]
MFCD00131472 |
| Hazard Information | Back Directory | [Uses]
L-Tyrosine decarboxylase from Streptococcus faecalis has been used in a study to isolate and identify the carbonyl-active site of diamine oxidase by gas chromatographic mass spectrometry. L-Tyrosine decarboxylase from Streptococcus faecalis has also been used in a study to investigate the adsorption of Streptococcus faecalis on diatomite carriers for use in biotransformations. | [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. |
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