Enzyme

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     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.1 Hydro-lyases
ID:4.2.1.20
Description:Tryptophan synthase.
Alternative Name: Tryptophan synthetase.
Tryptophan desmolase.
L-tryptophan synthetase.
Indoleglycerol phosphate aldolase.
Prosite: PDOC00152; PDOC00151;
PDB:
PDBScop
1WDW 8030882; 8043261; 8030882; 8043261; 8030882; 8043261; 8020673; 8033053; 8020673; 8033053; 8020673; 8033053; 8030882; 8043261; 8030882; 8043261; 8030882; 8043261; 8020673; 8033053; 8020673; 8033053; 8020673; 8033053;
6CUZ 8020673; 8033053; 8020673; 8033053; 8020673; 8033053; 8020673; 8033053;
6CUT 8020673; 8033053; 8020673; 8033053; 8020673; 8033053; 8020673; 8033053;
6AMH 8020673; 8033053; 8020673; 8033053; 8020673; 8033053; 8020673; 8033053;
6AM9 8020673; 8033053; 8020673; 8033053; 8020673; 8033053; 8020673; 8033053;
 » show all

Cath: 3.20.20.70; 3.30.429.10; 3.40.1030.10; 3.40.50.880; 3.60.120.10; 1.20.970.10; 3.40.50.1100;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.1.20
BRENDA Enzyme Link: BRENDA 4.2.1.20
KEGG Enzyme Link: KEGG4.2.1.20
BioCyc Enzyme Link: BioCyc 4.2.1.20
ExPASy Enzyme Link: ExPASy4.2.1.20
EC2PDB Enzyme Link: EC2PDB 4.2.1.20
ExplorEnz Enzyme Link: ExplorEnz 4.2.1.20
PRIAM enzyme-specific profiles Link: PRIAM 4.2.1.20
IntEnz Enzyme Link: IntEnz 4.2.1.20
MEDLINE Enzyme Link: MEDLINE 4.2.1.20
MSA:

4.2.1.20;

Phylogenetic Tree:

4.2.1.20;

Uniprot:
M-CSA:
RHEA:10532 (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
RULE(radius=1) [*:1]-[CH2;+0:2]-[OH;+0:3].[*:4]:[c;H0;+0:5](:[*:6])-[CH;+0:7](-[*:8])-[OH;+0:9]>>[*:8]-[CH;+0:7]=[O;H0;+0:9].[*:4]:[c;H0;+0:5](:[*:6])-[CH2;+0:2]-[*:1].[OH2;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Tryptophan biosynthetic genes in eukaryotic microorganisms.Hütter R, Niederberger P, DeMoss JA19863535653
Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium.Hyde CC, Ahmed SA, Padlan EA, Miles EW, Davies DR1988 Nov 253053720
ON THE SEPARATION OF THE TRYPTOPHAN SYNTHETASE OF ESCHERICHIA COLI INTO TWO PROTEIN COMPONENTS.Crawford IP, Yanofsky C1958 Dec 1516590328
Mechanisms of monovalent cation action in enzyme catalysis: the tryptophan synthase alpha-, beta-, and alpha beta-reactions.Woehl E, Dunn MF1999 Jun 110353823