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