CATH Classification

Domain Context

CATH Clusters

Superfamily Aspartate Aminotransferase, domain 1
Functional Family

Enzyme Information

4.1.99.1
Tryptophanase.
based on mapping to UniProt P28796
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)

P28796
TNAA_PROVU
Proteus vulgaris
Tryptophanase

PDB Structure

PDB 1AX4
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal structure of tryptophanase.
Isupov, M.N., Antson, A.A., Dodson, E.J., Dodson, G.G., Dementieva, I.S., Zakomirdina, L.N., Wilson, K.S., Dauter, Z., Lebedev, A.A., Harutyunyan, E.H.
J.Mol.Biol.