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Tryptophanase

An enzyme that catalyzes the conversion of L-tryptophan and water to indole, pyruvate, and ammonia. It is a pyridoxal-phosphate protein, requiring K+. It also catalyzes 2,3-elimination and beta-replacement reactions of some indole-substituted tryptophan analogs of L-cysteine, L-serine, and other 3-substituted amino acids. (From Enzyme Nomenclature, 1992) EC 4.1.99.1.
Also Known As:
Indole-Lyase, Tryptophan; Tryptophan Indole Lyase; Tryptophan Indole-Lyase; L-Tryptophan indole-lyase (deaminating)
Networked: 15 relevant articles (0 outcomes, 0 trials/studies)

Bio-Agent Context: Research Results

Experts

1. Anyanful, Akwasi: 2 articles (09/2011 - 08/2005)
2. Kalman, Daniel: 2 articles (09/2011 - 08/2005)
3. Abe, Takaaki: 1 article (01/2022)
4. Katayama, Takane: 1 article (01/2022)
5. Kikuchi, Koichi: 1 article (01/2022)
6. Nakayama, Toru: 1 article (01/2022)
7. Oikawa, Daiki: 1 article (01/2022)
8. Takahashi, Seiji: 1 article (01/2022)
9. Waki, Toshiyuki: 1 article (01/2022)
10. Yamashita, Satoshi: 1 article (01/2022)

Related Diseases

1. Carcinogenesis
2. Paralysis (Palsy)
3. Infections
4. Aberrant Crypt Foci
5. Chronic Renal Insufficiency

Related Drugs and Biologics

1. Enzymes
2. Glucuronidase
3. Urease
4. Tryptophan (L-Tryptophan)
5. indole
6. Membrane Transport Proteins (Biological Pump)
7. 1,2-Dimethylhydrazine (1,2 Dimethylhydrazine)
8. Aryl Hydrocarbon Receptors (Aryl Hydrocarbon Receptor)
9. Lignans
10. RNA-Binding Proteins (RNA-Binding Protein)