CATH Classification

Domain Context

CATH Clusters

Superfamily Aspartate Aminotransferase, domain 1
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 2C44
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structure of Escherichia Coli Tryptophanase
Ku, S.-Y., Yip, P., Howell, P.L.
Acta Crystallogr.,Sect.D
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