A6007
Apotryptophanase from Escherichia coli
soluble powder, 75-150 units/mg solid
别名:
Tryptophanase from Escherichia coli, L-Tryptophan indole-lyase (deaminating)
应用
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 .
生化/生理作用
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 .
其他说明
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.
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
常规特殊物品
此项目有
历史批次信息供参考:
分析证书(COA)
Lot/Batch Number
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
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
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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