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B6db activities: 4.1.99.1

4.1.99.1
Description Tryptophanase.
Alternative names L-tryptophan indole-lyase;
Tnase.
Catalyzed reaction L-tryptophan + H(2)O = indole + pyruvate + NH(3).
Cofactor Pyridoxal-phosphate; Potassium.
Comments -!- Also catalyzes the synthesis of tryptophan from indole and serine.
-!- 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.
-!-The E. coli enzyme shows a substantial L-cysteine desulfhydrase activity.
Indole, the product of this enzyme, is a signal molecule in Escherichia coli and other bacteria. In particular, it can slow down cell division and act as an extracellular signal to regulate biofilm formation.
Prosite PROSITE; PDOC00667;
PDB 1AX4; 2C44;
Organisms -Bacteria -Archea
 

Family 

4.1.99.1 (15)
 
Links Enzyme (activities) 4.1.99.1
BRENDA (activities) 4.1.99.1
KEGG (pathways) 4.1.99.1
PLPMDB (PLP mutants) 4.1.99.1
 
References
 Chant EL, Summers DK. (2007) Indole signalling contributes to the stable maintenance of Escherichia coli multicopy plasmids Mol Microbiol 63 35-43.

 Ku SY, Yip P, Howell PL. (2006) Structure of Escherichia coli tryptophanase Acta Crystallogr D Biol Crystallogr 62 814-23.

 Awano N, Wada M, Kohdoh A, Oikawa T, Takagi H, Nakamori S. (2003) Effect of cysteine desulfhydrase gene disruption on L-cysteine overproduction in Escherichia coli Appl Microbiol Biotechnol 62 239-43.

 Martino PD, Fursy R, Bret L, Sundararaju B, Phillips RS. (2003) Indole can act as an extracellular signal to regulate biofilm formation of Escherichia coli and other indole-producing bacteria Can J Microbiol 49 443-9.

 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. (1998) Crystal structure of tryptophanase J Mol Biol 276 603-23.

 Martin, K.; Morlin, G.; Smith, A.; Nordyke, A.; Eisenstark, A.; Golomb, M. (1998) The tryptophanase gene cluster of Haemophilus influenzae type b: evidence for horizontal gene transfer J Bacteriol 180 107-18.

 Kawasaki K, Yokota A, Tomita F. (1995) Enzymatic synthesis of L-tryptophan by Enterobacter aerogenes tryptophanase highly expressed in Escherichia coli, and some properties of the purified enzyme Biosci Biotechnol Biochem 59 1938-43.

 Kawasaki, K.; Yokota, A.; Oita, S.; Kobayashi, C.; Yoshikawa, S.; Kawamoto, S.; Takao, S.; Tomita, F. (1993) Cloning and characterization of a tryptophanase gene from Enterobacter aerogenes SM-18 J Gen Microbiol 235139 3275-81.

 Hirahara, T.; Suzuki, S.; Horinouchi, S.; Beppu, T. (1992) Cloning, nucleotide sequences, and overexpression in Escherichia coli of tandem copies of a tryptophanase gene in an obligately symbiotic thermophile, Symbiobacterium thermophilum Appl Environ Microbiol 58 2633-42.

 Deeley, M.C.; Yanofsky, C. (1981) Nucleotide sequence of the structural gene for tryptophanase of Escherichia coli K-12 J Bacteriol 147 787-96.

Articles on 4.1.99.1
 
last changed 2009/07/10 16:44

B6db activities