MetaCyc Reaction:

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:

Enzymes and Genes:

Escherichia coli K-12 substr. MG1655 : tryptophan synthase Inferred from experiment : trpA , trpB
Thermococcus kodakarensis : tryptophan synthase complex Inferred from experiment : trpA , trpB
Thermotoga maritima : tryptophan synthase : trpA , trpB1

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: tryptophan synthase

Enzyme Commission Synonyms: L-tryptophan synthetase, indoleglycerol phosphate aldolase, tryptophan desmolase, tryptophan synthetase, L-serine hydro-lyase (adding indoleglycerol-phosphate), L-serine hydro-lyase [adding 1-C-(indol-3-yl)glycerol 3-phosphate, L-tryptophan and glyceraldehyde-3-phosphate-forming]

Taxonomic Range: Fungi , Viridiplantae , Archaea , Bacteria

(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate ↔ indole + D-glyceraldehyde 3-phosphate ,
L-serine + indole → L-tryptophan + H2O

Standard Gibbs Free Energy (ΔrG in kcal/mol): 11.682007 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
A pyridoxal-phosphate protein. The α-subunit catalyses the conversion of 1-C-(indol-3-yl)glycerol 3-phosphate to indole and glyceraldehyde 3-phosphate (this reaction was listed formerly as EC The indole migrates to the β-subunit where, in the presence of pyridoxal 5'-phosphate, it is combined with L-serine to form L-tryptophan. In some organisms this enzyme is part of a multifunctional protein that also includes one or more of the enzymes EC (anthranilate phosphoribosyltransferase), EC (indole-3-glycerol-phosphate synthase), EC (anthranilate synthase) and EC (phosphoribosylanthranilate isomerase). In thermophilic organisms, where the high temperature enhances diffusion and causes the loss of indole, a protein similar to the α subunit can be found (EC That enzyme cannot combine with the β unit of EC to form a complex.

Citations: [Crawford58, Hutter86, Hyde88, Woehl99]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Unification Links: KEGG:R02722 , Rhea:10532

Relationship Links: BRENDA:EC: , ENZYME:EC: , IUBMB-ExplorEnz:EC: , UniProt:RELATED-TO:O04225 , UniProt:RELATED-TO:O05625 , UniProt:RELATED-TO:O13831 , UniProt:RELATED-TO:O22765 , UniProt:RELATED-TO:O27696 , UniProt:RELATED-TO:O28672 , UniProt:RELATED-TO:O64991 , UniProt:RELATED-TO:O66923 , UniProt:RELATED-TO:O84172 , UniProt:RELATED-TO:P00929 , UniProt:RELATED-TO:P00931 , UniProt:RELATED-TO:P06561 , UniProt:RELATED-TO:P06562 , UniProt:RELATED-TO:P07600 , UniProt:RELATED-TO:P07601 , UniProt:RELATED-TO:P0A2K1 , UniProt:RELATED-TO:P0A877 , UniProt:RELATED-TO:P0A879 , UniProt:RELATED-TO:P11080 , UniProt:RELATED-TO:P11081 , UniProt:RELATED-TO:P12290 , UniProt:RELATED-TO:P12291 , UniProt:RELATED-TO:P13228 , UniProt:RELATED-TO:P14671 , UniProt:RELATED-TO:P16578 , UniProt:RELATED-TO:P16608 , UniProt:RELATED-TO:P16706 , UniProt:RELATED-TO:P17166 , UniProt:RELATED-TO:P17167 , UniProt:RELATED-TO:P18284 , UniProt:RELATED-TO:P18285 , UniProt:RELATED-TO:P19867 , UniProt:RELATED-TO:P19868 , UniProt:RELATED-TO:P25269 , UniProt:RELATED-TO:P31204 , UniProt:RELATED-TO:P34793 , UniProt:RELATED-TO:P34816 , UniProt:RELATED-TO:P34817 , UniProt:RELATED-TO:P42389 , UniProt:RELATED-TO:P42390 , UniProt:RELATED-TO:P42391 , UniProt:RELATED-TO:P43283 , UniProt:RELATED-TO:P43284 , UniProt:RELATED-TO:P43759 , UniProt:RELATED-TO:P43760 , UniProt:RELATED-TO:P50909 , UniProt:RELATED-TO:P51382 , UniProt:RELATED-TO:P56142 , UniProt:RELATED-TO:P77960 , UniProt:RELATED-TO:Q9JVC0 , UniProt:RELATED-TO:Q9PIF1 , UniProt:RELATED-TO:Q9PIF2 , UniProt:RELATED-TO:Q9X7C8 , UniProt:RELATED-TO:Q9YGA9 , UniProt:RELATED-TO:Q9YGB0 , UniProt:RELATED-TO:Q01997 , UniProt:RELATED-TO:Q01998 , UniProt:RELATED-TO:Q42529 , UniProt:RELATED-TO:Q57011 , UniProt:RELATED-TO:Q59992 , UniProt:RELATED-TO:Q60179

Revised 25-Aug-2011 by Caspi R , SRI International


Crawford58: Crawford IP, Yanofsky C (1958). "On the separation of the tryptophan synthetase of Escherichia coli into two protein components." Proc Natl Acad Sci U S A 44(12);1161-70. PMID: 16590328

Hutter86: Hutter R, Niederberger P, DeMoss JA (1986). "Tryptophan biosynthetic genes in eukaryotic microorganisms." Annu Rev Microbiol 40;55-77. PMID: 3535653

Hyde88: Hyde CC, Ahmed SA, Padlan EA, Miles EW, Davies DR (1988). "Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium." J Biol Chem 263(33);17857-71. PMID: 3053720

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

Woehl99: Woehl E, Dunn MF (1999). "Mechanisms of monovalent cation action in enzyme catalysis: the tryptophan synthase alpha-, beta-, and alpha beta-reactions." Biochemistry 38(22);7131-41. PMID: 10353823

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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 19.0 on Sun Oct 4, 2015, biocyc13.