Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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MetaCyc Reaction: 4.1.99.1

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions Composite Reactions
Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 4.1.99.1

Enzymes and Genes:
tryptophanase / L-cysteine desulfhydrase : tnaA ( Escherichia coli K-12 substr. MG1655 )
tryptophanase : tna1 ( Symbiobacterium thermophilum )
tryptophanase ( Paenibacillus alvei )
tryptophanase : tnaA ( Enterobacter aerogenes )

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: Balanced.

Enzyme Commission Primary Name: tryptophanase

Enzyme Commission Synonyms: L-tryptophanase, L-tryptophan indole-lyase (deaminating)

Sub-reactions:
L-tryptophan ↔ indole + 2-aminoprop-2-enoate + H+ ,
2-aminoprop-2-enoate → 2-iminopropanoate ,
2-iminopropanoate + H+ + H2O → pyruvate + ammonium

Standard Gibbs Free Energy (ΔrG in kcal/mol): 5.1028786 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
A pyridoxal-phosphate protein, requiring K+. Also catalyses 2,3-elimination and β-replacement reactions of some indole-substituted tryptophan analogues of L-cysteine, L-serine and other 3-substituted amino acids.

Citations: [Newton65, Burns62]

Unification Links: KEGG:R00673 , Rhea:19553

Relationship Links: BRENDA:EC:4.1.99.1 , ENZYME:EC:4.1.99.1 , IUBMB-ExplorEnz:EC:4.1.99.1 , UniProt:RELATED-TO:P0A853 , UniProt:RELATED-TO:P28796 , UniProt:RELATED-TO:P31014 , UniProt:RELATED-TO:P31015


References

Burns62: Burns RO, Demoss RD (1962). "Properties of tryptophanase from Escherichia coli." Biochim Biophys Acta 65;233-44. PMID: 14017164

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Newton65: Newton WA, Morino Y, Snell EE (1965). "Properties of crystalline tryptophanase." J Biol Chem 240;1211-8. PMID: 14284727


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sun Dec 21, 2014, BIOCYC13A.