tryptophanase

tryptophanase

 [trip´to-fan″ās]
an enzyme that catalyzes the cleavage of tryptophan into indole, pyruvic acid, and ammonia.

tryp·to·pha·nase

(trip'to-fă-nās),
1. Synonym(s): tryptophan 2, 3-dioxygenase
2. An enzyme found in bacteria that catalyzes the cleavage of l-tryptophan to indole, pyruvic acid, and ammonia; pyridoxal phosphate is a coenzyme.

tryptophanase

(1) Tryptophan 2,3-dioxygenase, EC 1.13.11.11.
(2) Tryptophanase, EC 4.1.99.1.

tryp·to·pha·nase

(trip'tō-fă-nās)
1. Synonym(s): tryptophan 2, 3-dioxygenase.
2. An enzyme found in bacteria that catalyzes the cleavage of l-tryptophan to indole, pyruvic acid, and ammonia; pyridoxal phosphate is a coenzyme.

tryptophanase

an enzyme that catalyzes the cleavage of tryptophan into indole, pyruvic acid and ammonia.
References in periodicals archive ?
Likewise, tryptophanase was also significantly downregulated in male animals but not in females (Figure 3D).
pneumoniae which show negative reaction because they are non motile and can not produce tryptophanase enzyme as well as does not reduce sodium thiosulphate in the medium (Table 1).
A colorimetric method for the determination of indole, and its application to assay of tryptophanase.
Kinetics of L-tryptophan production from indole and L-serine catalyzed by whole cells with tryptophanase activity.
The essential amino acid tryptophan has been hypothesized to be the ultimate precursor for indole production, in which tryptophanase enzymes act on tryptophan to produce indoles (Verhecken 1989, Naegel & Alvarez 2005, Westley et al.
Indole biosynthesis can be detected in microbial communities using biochemical tests such as the indole (tryptophan degradation) test and tryptophanase activity (Holding & Collee 1971, Lammert 2007).
The production of tryptophanase, sufficient amount of alcohol, acetyl methyl carbinol, and citrate utilisation were noted using the indole test, methyl red (MR) test, Voges-Proskauer (VP) test, and citrate utilization test, respectively, according to the protocol of Mackie McCartney [14].
tryptophan for detection of tryptophanase activity (indole production) and of tryptophan deaminase activity.
Tryptophanase operon (tnaOP) is a region consisting of two major structural genes: tnaA, coding for the tryptophanase which catalyzes the degradation of L-tryptophan to indole, pyruvate, and ammonia and tnaB coding for a tryptophan permease.
The following were chosen from the small chromosome: dtdS, the encoding threonine dehydrogenase; lysA, the encoding diaminopimelate decarboxylase; pntA, the encoding transhydrogenase alpha sub-unit; pyrC, the encoding dihydroorotase; and tnaA, the encoding tryptophanase.
coli the environmental conditions of the intestine induce the expression of tryptophanase (tnaA), the enzyme that generates indole.
For example Sequences from the uidA [4], coding for GUD, gadA/B [7], coding for GAD, tna, coding for tryptophanase operon [5] and cadA, coding for lysine decarboxylase [13] are reported repetitively as applicable tools for tracing E.