WebTryptophanase. 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 … WebApr 1, 1999 · 4.1.99.1 tryptophanase. IUBMB Comments. A pyridoxal-phosphate protein, requiring K+. The enzyme cleaves a carbon-carbon bond, releasing indole and an unstable …
Tryptophanase - an overview ScienceDirect Topics
WebJun 10, 2024 · Tryptophanase is an intracellular enzyme, which catalyzes the breakdown of the amino acid tryptophan to pyruvate and indole. The pyruvate is used by the cell as a … WebAug 10, 2024 · Tryptophan is an amino acid that can undergo deamination and hydrolysis by bacteria that express tryptophanase enzyme. Indole is generated by reductive deamination from tryptophan via the intermediate … csfd bambinot
Tryptophanase - WikiMili, The Best Wikipedia Reader
WebStructure and Evolution of a Bifunctional Enzyme of the Tryptophan Operon. MANFRED GRIESHABER &. RONALD BAUERLE. Nature New Biology 236 , 232–235 ( 1972) Cite this … WebJun 7, 2005 · Status. UniProtKB reviewed (Swiss-Prot) Organism. Escherichia coli (strain K12) Amino acids. 471. Protein existence. Evidence at protein level. Annotation score. The enzyme tryptophanase (EC 4.1.99.1) catalyzes the chemical reaction L-tryptophan + H2O $${\displaystyle \rightleftharpoons }$$ indole + pyruvate + NH3This enzyme belongs to the family of lyases, specifically in the "catch-all" class of carbon-carbon lyases. The systematic name of this enzyme class is L-tryptophan … See more As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1AX4, 2C44, and 2OQX. See more • Media related to Tryptophanase at Wikimedia Commons See more csfd anthony hopkins