CATH Classification

Domain Context

CATH Clusters

Superfamily Type I PLP-dependent aspartate aminotransferase-like (Major domain)
Functional Family Tryptophanase

Enzyme Information

4.1.99.1
Tryptophanase.
based on mapping to UniProt P0A853
L-tryptophan + H(2)O = indole + pyruvate + NH(3).
-!- The enzyme cleaves a carbon-carbon bond, releasing indole and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. -!- The latter reaction, which can occur spontaneously, can also be catalyzed by EC 3.5.99.10. -!- 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.

UniProtKB Entries (1)

P0A853
TNAA_ECOLI
Escherichia coli K-12
Tryptophanase

PDB Structure

PDB 4W4H
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structures of Escherichia coli tryptophanase in holo and `semi-holo' forms.
Kogan, A., Raznov, L., Gdalevsky, G.Y., Cohen-Luria, R., Almog, O., Parola, A.H., Goldgur, Y.
Acta Crystallogr.,Sect.F