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1WDW;
2E09;
2DZX;
2DZW;
2DZV;
2DZU;
2DZT;
2DZS;
2DZP;
1GEQ;
1TJR;
1RD5;
5E0K;
4ZQC;
4HT3;
4HPX;
4HPJ;
2TYS;
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;
2TSY;
2TRS;
2RH9;
2J9Z;
2J9Y;
2CLM;
2CLL;
2CLK;
2CLI;
2CLH;
1WBJ;
1UBS;
1TTQ;
1TTP;
1TJP;
1QOQ;
1KFK;
1KFJ;
1KFE;
1K8Z;
1K8Y;
1K7F;
1CX9;
1CW2;
1C9D;
1C8V;
1BKS;
1A50;
6QKY;
6HUL;
6E9P;
6DWE;
6DUA;
6DU1;
5TCJ;
5TCI;
5TCH;
5TCG;
5TCF;
5OCW;
5N2P;
5KZM;
5KIN;
3THA;
3NAV;
2EKC;
1K7E;
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UniProtKB Enzyme Link: | UniProtKB 4.1.2.8 |
BRENDA Enzyme Link: | BRENDA 4.1.2.8 |
KEGG Enzyme Link: | KEGG4.1.2.8 |
BioCyc Enzyme Link: | BioCyc 4.1.2.8 |
ExPASy Enzyme Link: | ExPASy4.1.2.8 |
EC2PDB Enzyme Link: | EC2PDB 4.1.2.8 |
ExplorEnz Enzyme Link: | ExplorEnz 4.1.2.8 |
PRIAM enzyme-specific profiles Link: | PRIAM 4.1.2.8 |
IntEnz Enzyme Link: | IntEnz 4.1.2.8 |
MEDLINE Enzyme Link: | MEDLINE 4.1.2.8 |
RHEA:14081 | (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = D-glyceraldehyde 3-phosphate + indole |
RULE(radius=1) | [*:1]:[c;H0;+0:2](:[*:3])-[CH;+0:4](-[*:5])-[OH;+0:6]>>[*:5]-[CH;+0:4]=[O;H0;+0:6].[*:1]:[cH;+0:2]:[*:3] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
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 |
Proteomic survey of copper-binding proteins in Arabidopsis roots by immobilized metal affinity chromatography and mass spectrometry. | Kung CC, Huang WN, Huang YC, Yeh KC | 2006 May | 16526091 |
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 |