A6007
Apotryptophanase from Escherichia coli
soluble powder, 75-150 units/mg solid
Sinónimos:
Tryptophanase from Escherichia coli, L-Tryptophan indole-lyase (deaminating)
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Número CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
75-150 units/mg solid
Biological source:
Escherichia coli
Servicio técnico
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Permítanos ayudarlebiological source
Escherichia coli
Quality Level
form
soluble powder
specific activity
75-150 units/mg solid
storage temp.
−20°C
Application
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 .
Biochem/physiol Actions
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 .
Other Notes
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.
Clase de almacenamiento
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Anna Kogan et al.
BMC structural biology, 9, 65-65 (2009-10-10)
Oligomeric enzymes can undergo a reversible loss of activity at low temperatures. One such enzyme is tryptophanase (Trpase) from Escherichia coli. Trpase is a pyridoxal phosphate (PLP)-dependent tetrameric enzyme with a Mw of 210 kD. PLP is covalently bound through
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Zuzana Zubáčová et al.
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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