A6007
Apotryptophanase from Escherichia coli
soluble powder, 75-150 units/mg solid
Synonym(s):
Tryptophanase from Escherichia coli, L-Tryptophan indole-lyase (deaminating)
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
75-150 units/mg solid
Biological source:
Escherichia coli
biological source
Escherichia coli
form
soluble powder
specific activity
75-150 units/mg solid
storage temp.
−20°C
Quality Level
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.
Storage Class
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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Christian Starkenmann et al.
Journal of agricultural and food chemistry, 59(7), 3358-3365 (2011-03-08)
The objective of this study was to verify whether the volatile organic sulfur compounds recently discovered in bell pepper (Capsicum annuum, L. cultivars), such as the mercapto-ketones: 4-sulfanyl-2-heptanone and 2-sulfanyl-4-heptanone, the mercapto-alcohols: 4-sulfanyl-2-heptanol and 2-sulfanyl-4-heptanol, and heptane-2,4-dithiol, originate from their
Dorota Kuczyńska-Wiśnik et al.
Research in microbiology, 161(10), 847-853 (2010-09-28)
Recent studies have revealed that antibiotics can promote the formation of reactive oxygen species which contribute to cell death. In this study, we report that five different antibiotics known to stimulate production of reactive oxygen species inhibited growth of Escherichia
Leonardo G Trabuco et al.
Structure (London, England : 1993), 18(5), 627-637 (2010-05-14)
Regulatory nascent chains interact with the ribosomal exit tunnel and modulate their own translation. To characterize nascent chain recognition by the ribosome at the atomic level, extensive molecular dynamics simulations of TnaC, the leader peptide of the tryptophanase operon, inside
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
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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