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A6007

Sigma-Aldrich

Apotryptophanase from Escherichia coli

soluble powder, 75-150 units/mg solid

Sinonimo/i:

Tryptophanase from Escherichia coli, L-Tryptophan indole-lyase (deaminating)

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About This Item

Numero CAS:
9024-00-4
Classificazione EC (Enzyme Commission):
4.1.99.1 (BRENDA, IUBMB)
Numero MDL:
MFCD00130539
Codice UNSPSC:
12352204
NACRES:
NA.54

Origine biologica

Escherichia coli

Livello qualitativo

200

Forma fisica

soluble powder

Attività specifica

75-150 units/mg solid

Temperatura di conservazione

−20°C

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Applicazioni

Apotryptophanase is used for the quantitative determination of pyridoxal-phosphate. Apotryptophanase, from Sigma, has been used to study pregnancy-associated PLP deficiency and vitamin B-6 deficiency .

Azioni biochim/fisiol

Apotryptophanase hydrolizes tryptophan and is capable of catalyzing α,β-elimination reactions with a number of substituted amino acids, including S-methyl-, S-ethyl- and S-benzyl- L-cysteine. DTNB inactivates tryptophanase .

Definizione di unità

One unit releases one μg of indole from L-tryptophan in 10 min at pH 8.3 at 37 °C in the presence of 0.04 mM pyridoxal-5′--phosphate.

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)

Certificati d'analisi (COA)

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Birgit Seidelt et al.
Science (New York, N.Y.), 326(5958), 1412-1415 (2009-11-26)
Expression of the Escherichia coli tryptophanase operon depends on ribosome stalling during translation of the upstream TnaC leader peptide, a process for which interactions between the TnaC nascent chain and the ribosomal exit tunnel are critical. We determined a 5.8
Elzbieta Winnicka et al.
Isotopes in environmental and health studies, 46(2), 225-232 (2010-06-29)
The kinetic and solvent deuterium isotope effects in the 4- and 5-positions of the indole ring on the enzymatic decomposition of l-tryptophan catalysed by the enzyme TPase (EC. 4.1.99.1) were determined. The isotope effects were investigated by the non-competitive method
Zuzana Zubáčová et al.
Molecular and biochemical parasitology, 176(2), 135-137 (2011-01-05)
The highly repetitive nature of the Trichomonas vaginalis genome and massive expansion of various gene families has caused difficulties in genome assembly and has hampered genome mapping. Here, we adapted fluorescence in situ hybridization (FISH) for T. vaginalis, which is
Takako Sasaki-Imamura et al.
Applied and environmental microbiology, 76(13), 4260-4268 (2010-05-18)
The l-tryptophan degradation product indole is a purported extracellular signaling molecule that influences biofilm formation in various bacteria. Here we analyzed the mechanisms of indole production in Fusobacterium nucleatum and the effects of tryptophan and indole on F. nucleatum planktonic
Nicholas S Wigginton et al.
Environmental science & technology, 44(6), 2163-2168 (2010-02-18)
Here we describe results from a proteomic study of protein-nanoparticle interactions to further the understanding of the ecotoxicological impact of silver nanoparticles (AgNPs) in the environment. We identified a number of proteins from Escherichia coli that bind specifically to bare
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