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Acta Crystallographica Section D, ISSN 2059-7983, 08/2018, Volume 74, Issue 8, pp. 748 - 759
Journal Article
ACTA NATURAE, ISSN 2075-8251, 07/2019, Volume 11, Issue 3, pp. 82 - 88
In the reaction between tryptophan indole-lyase (TIL) and a substrate containing a bad leaving group (L-serine), general acid catalysis is required for the... 
ANALOGS | TYROSINE PHENOL-LYASE | CRYSTAL-STRUCTURE | ESCHERICHIA-COLI | tryptophan indole-lyase | beta-chloro-L-alanine | OXINDOLYL-L-ALANINE | CELL BIOLOGY | L-serine | INTERMEDIATE | PYRIDOXAL-PHOSPHATE | STEADY-STATE | INHIBITORS | mechanism | kinetics | β-chloro-L-alanine
Journal Article
Protein Science, ISSN 0961-8368, 04/2004, Volume 13, Issue 4, pp. 913 - 924
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 02/2000, Volume 122, Issue 6, pp. 1008 - 1014
Tryptophan indole-lyase from Escherichia coli catalyzes the reversible cleavage of l-tryptophan to indole and ammonium pyruvate. This reaction is... 
SYNTHASE | ENZYME | MECHANISM | ACTIVE-SITE | ANALOGS | 2,3-DIHYDRO-L-TRYPTOPHAN | STEREOCHEMISTRY | INTERMEDIATE | PYRIDOXAL-PHOSPHATE | CHEMISTRY, MULTIDISCIPLINARY | NUCLEOTIDE-SEQUENCE | Tryptophan | Scission (Chemistry) | Research
Journal Article
The FEBS journal, 04/2013, Volume 280, Issue 8, p. 1807
Tryptophan indole lyase (TIL), an enzyme found in Escherichia coli and related enterobacteria, produces indole from l-tryptophan (l-Trp). Indole is a signaling... 
Escherichia coli - enzymology | Tryptophan - analogs & derivatives | Benzimidazoles - chemical synthesis | Enzyme Inhibitors - pharmacology | Benzimidazoles - pharmacology | Tryptophanase - antagonists & inhibitors | Kinetics | Enzyme Inhibitors - chemical synthesis | Tryptophanase - metabolism
Journal Article
Journal of Inclusion Phenomena and Macrocyclic Chemistry, ISSN 0923-0750, 4/2006, Volume 54, Issue 3, pp. 283 - 288
Journal Article
Scientific Reports, ISSN 2045-2322, 12/2018, Volume 8, Issue 1, pp. 2659 - 9
Genetic circuit-based biosensors are useful in detecting target metabolites or in vivo enzymes using transcription factors (Tx) as a molecular switch to... 
INACTIVATION | TRYPTOPHAN INDOLE-LYASE | MECHANISM | ACTIVE-SITE | TYROSINE PHENOL-LYASE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | PROTEIN DESIGN | DIRECTED EVOLUTION | Tyrosine | Flow cytometry | Enzymes | Transcription factors | Indole | Tryptophan | High-throughput screening | Phenolic compounds | Metabolites | Antibiotic resistance | Phenols | Mutation | Biosensors
Journal Article
ACS Catalysis, ISSN 2155-5435, 10/2016, Volume 6, Issue 10, pp. 6770 - 6779
The role of transition-state stabilization in enzyme catalysis, as proposed by Pauling, has been clearly demonstrated by extensive studies. In contrast,... 
pyridoxal-5′-phosphate | rate acceleration | ground-state strain | enzyme mechanism | kinetics | TRYPTOPHAN INDOLE-LYASE | SPECIFICITY | CHEMISTRY, PHYSICAL | pyridoxal-5 '-phosphate | SITE-DIRECTED MUTAGENESIS | SUBSTRATE DISTORTION | EQUILIBRIA | REACTION-MECHANISM | OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE | X-RAY | BINDING | STRAIN
Journal Article