4.1.99.1: tryptophanase

This is an abbreviated version!
For detailed information about tryptophanase, go to the full flat file.

Word Map on EC 4.1.99.1

4.1.99.1

quinonoid

transposase

aldimine

proteus

phenol-lyase

thermonuclease

beta-elimination

l-trp

tryptophan-induced

antitermination

pyridoxal-p

rho-dependent

rapid-scanning

phillips

alvei

analysis

food industry

biotechnology

drug development

medicine

synthesis

Reaction

Synonyms

L-tryptophan indole-lyase, L-tryptophanase, TIL, tna2, TnaA, tnaA2, TNase, Tpase, Trpase, tryptophan indole lyase, tryptophan indole-lyase, tryptophan-indole lyase, tryptophanase, tryptophanase 2, VcTrpase

ECTree

4 Lyases

4.1 Carbon-carbon lyases

4.1.99 Other carbon-carbon lyases

4.1.99.1 tryptophanase

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Results	in table
8	Activating Compound
2608	AA Sequence
7	Application
1	CAS Registry Number
19	Cloned(Commentary)
67	Cofactor
15	Crystallization (Commentary)
82	Disease/ Diagnostics
8	Expression
26	General Information
6	General Stability
76	Inhibitors
30	kcat/KM [mM/s]
33	Ki Value [mM]
88	KM Value [mM]
45	Metals/Ions
32	Molecular Weight [Da]
36	Natural Substrates/ Products (Substrates)
799	Organism
4	Pathway
28	PDB ID
23	pH Optimum
3	pH Range
2	pH Stability
1	pI Value
86	Protein Variants
28	Purification (Commentary)
15	Reaction
5	Reaction Type
161	Reference
1	Renatured (Commentary)
5	Source Tissue
20	Specific Activity [micromol/min/mg]
4	Storage Stability
288	Substrates and Products (Substrate)
47	Subunits
84	Synonyms
1	Systematic Name
10	Temperature Optimum [°C]
1	Temperature Range [°C]
24	Temperature Stability [°C]
39	Turnover Number [1/s]

Systematic Name

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Systematic Name on EC 4.1.99.1 - tryptophanase

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L-tryptophan indole-lyase (deaminating; pyruvate-forming)

A pyridoxal-phosphate protein, requiring K+. 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 catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. Also catalyses 2,3-elimination and beta-replacement reactions of some indole-substituted tryptophan analogues of L-cysteine, L-serine and other 3-substituted amino acids.