Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 4.2.1.20

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

EC Number: 4.2.1.20

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

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 synθse, indoleglycerol phosphate aldolase, tryptophan desmolase, tryptophan synθse, 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]

Sub-reactions:
(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 [Latendresse, 2013]

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 4.1.2.8). 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 2.4.2.18 (anthranilate phosphoribosyltransferase), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate synthase) and EC 5.3.1.24 (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 4.2.1.122). That enzyme cannot combine with the β unit of EC 4.2.1.20 to form a complex.

Citations: [Crawford58, Hutter86, Hyde88, Woehl99]

Gene-Reaction Schematic: ?

Unification Links: KEGG:R02722 , Rhea:10532

Relationship Links: BRENDA:EC:4.2.1.20 , ENZYME:EC:4.2.1.20 , IUBMB-ExplorEnz:EC:4.2.1.20 , 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

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


References

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

Latendresse, 2013: 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


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 Sat Nov 22, 2014, BIOCYC14B.