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A6007

Sigma-Aldrich

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:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

Escherichia coli

Quality Level

form

soluble powder

specific activity

75-150 units/mg solid

storage temp.

−20°C

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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 .

Unit Definition

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 Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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
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
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

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