A6007
Apotryptophanase from Escherichia coli
soluble powder, 75-150 units/mg solid
别名:
Tryptophanase from Escherichia coli, L-Tryptophan indole-lyase (deaminating)
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化学文摘社编号:
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.
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
常规特殊物品
此项目有
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
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
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
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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