tryptophanase

tryptophanase

 [trip´to-fan″ās]
an enzyme that catalyzes the cleavage of tryptophan into indole, pyruvic acid, and ammonia.
Miller-Keane Encyclopedia and Dictionary of Medicine, Nursing, and Allied Health, Seventh Edition. © 2003 by Saunders, an imprint of Elsevier, Inc. All rights reserved.

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.
Farlex Partner Medical Dictionary © Farlex 2012

tryptophanase

(1) Tryptophan 2,3-dioxygenase, EC 1.13.11.11.
(2) Tryptophanase, EC 4.1.99.1.
Segen's Medical Dictionary. © 2012 Farlex, Inc. All rights reserved.

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.
Medical Dictionary for the Health Professions and Nursing © Farlex 2012
References in periodicals archive ?
Each biochemical test was done with known controls.11 Indole Production (IP) test was done in which bacteria split amino acid tryptophan into indole and pyruvic acid using the enzyme tryptophanase. Ehrlich reagent containing an aldehyde was used to detect indole production.
Indole catabolism is supported by tryptophanase, which can be induced by tryptophan or suppressed by glucose.
Snell, "Formation and interrelationships of tryptophanase and tryptophan synthetases in Escherichia coli," Journal of Bacteriology, vol.
coli by disrupting indole signaling, which is increased as a result of high tryptophanase expression [44].
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. Anal Biochem 1978;86:457-462.
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.
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.
Also, it was catalase, oxidase, caseinase, and tryptophanase positive.