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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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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
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Caulobacter crescentus CB15 Reaction: 4.2.1.20

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: 4.2.1.20

Enzymes and Genes:
tryptophan synthase : trpA , trpB

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 ,
indole + L-serine → L-tryptophan + H2O

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: ?

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


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

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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