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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: 9 relevant articles (0 outcomes, 0 trials/studies)

Bio-Agent Context: Research Results

Experts

1. Kalman, Daniel: 2 articles (09/2011 - 08/2005)
2. Anyanful, Akwasi: 2 articles (09/2011 - 08/2005)
3. Sherchand, Shardulendra P: 1 article (01/2014)
4. Zea, Arnold H: 1 article (01/2014)
5. Buckner, Lyndsey R: 1 article (01/2014)
6. Quayle, Alison J: 1 article (01/2014)
7. Chang, Theresa L: 1 article (01/2014)
8. Aiyar, Ashok: 1 article (01/2014)
9. Belland, Robert J: 1 article (01/2014)
10. Martin, David H: 1 article (01/2014)

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1. Paralysis (Palsy)
2. Infection
3. Aberrant Crypt Foci
4. Bacterial Vaginosis
5. Starvation

Related Drugs and Biologics

1. Enzymes
2. 1,2-Dimethylhydrazine (1,2 Dimethylhydrazine)
3. RNA-Binding Proteins (RNA-Binding Protein)
4. Urease
5. Tryptophan (L-Tryptophan)
6. L-Serine Dehydratase (Serine Dehydratase)
7. RNA (Ribonucleic Acid)
8. Peptide Elongation Factor Tu (EF-Tu)
9. Dihydrolipoamide Dehydrogenase (Lipoamide Dehydrogenase)
10. Glucuronidase