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1WDW;
6CUZ;
6CUT;
6AMH;
6AM9;
6AM8;
5VM5;
5DW0;
1V8Z;
4ZQC;
4HT3;
4HPX;
4HPJ;
2WSY;
2RHG;
2J9X;
2CLO;
2CLF;
2CLE;
1QOP;
1KFC;
1KFB;
1K8X;
1K7X;
1K3U;
1FUY;
1C29;
1A5S;
6D0V;
6C73;
5CGQ;
5BW6;
4Y6G;
4XUG;
4WX2;
4KKX;
4HN4;
3PR2;
3CEP;
2RH9;
2J9Z;
2J9Y;
2CLM;
2CLL;
2CLK;
2CLI;
2CLH;
1WBJ;
1TTQ;
1TTP;
1TJP;
1QOQ;
1KFK;
1KFJ;
1KFE;
1K8Z;
1K8Y;
1K7F;
1CX9;
1CW2;
1C9D;
1C8V;
1BKS;
1BEU;
1A5B;
1A5A;
1A50;
6HUL;
6HTE;
6EQN;
6DWE;
6DUA;
5TCJ;
5TCG;
5OCW;
4QYS;
4NEG;
2O2J;
2O2E;
2DH6;
2DH5;
1X1Q;
1K7E;
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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 |
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 |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Tryptophan biosynthetic genes in eukaryotic microorganisms. | Hütter R, Niederberger P, DeMoss JA | 1986 | 3535653 |
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 DR | 1988 Nov 25 | 3053720 |
ON THE SEPARATION OF THE TRYPTOPHAN SYNTHETASE OF ESCHERICHIA COLI INTO TWO PROTEIN COMPONENTS. | Crawford IP, Yanofsky C | 1958 Dec 15 | 16590328 |
Mechanisms of monovalent cation action in enzyme catalysis: the tryptophan synthase alpha-, beta-, and alpha beta-reactions. | Woehl E, Dunn MF | 1999 Jun 1 | 10353823 |