Enzyme

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     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.1 Hydro-lyases
ID:4.2.1.122
Description:Tryptophan synthase (indole-salvaging).
Alternative Name: Tryptophan synthase beta-2.
Cath: 3.20.20.70; 3.40.50.1100;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.1.122
BRENDA Enzyme Link: BRENDA 4.2.1.122
KEGG Enzyme Link: KEGG4.2.1.122
BioCyc Enzyme Link: BioCyc 4.2.1.122
ExPASy Enzyme Link: ExPASy4.2.1.122
EC2PDB Enzyme Link: EC2PDB 4.2.1.122
ExplorEnz Enzyme Link: ExplorEnz 4.2.1.122
PRIAM enzyme-specific profiles Link: PRIAM 4.2.1.122
IntEnz Enzyme Link: IntEnz 4.2.1.122
MEDLINE Enzyme Link: MEDLINE 4.2.1.122
MSA:

4.2.1.122;

Phylogenetic Tree:

4.2.1.122;

Uniprot:
M-CSA:
RHEA:26434 indole + L-serine = H2O + L-tryptophan
RULE(radius=1) [*:1]-[CH2;+0:2]-[OH;+0:3].[*:4]:[cH;+0:5]:[*:6]>>[*:1]-[CH2;+0:2]-[c;H0;+0:5](:[*:4]):[*:6].[OH2;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed 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 DR1988 Nov 253053720
ON THE SEPARATION OF THE TRYPTOPHAN SYNTHETASE OF ESCHERICHIA COLI INTO TWO PROTEIN COMPONENTS.Crawford IP, Yanofsky C1958 Dec 1516590328
Proteomic survey of copper-binding proteins in Arabidopsis roots by immobilized metal affinity chromatography and mass spectrometry.Kung CC, Huang WN, Huang YC, Yeh KC2006 May16526091
Mechanisms of monovalent cation action in enzyme catalysis: the tryptophan synthase alpha-, beta-, and alpha beta-reactions.Woehl E, Dunn MF1999 Jun 110353823
A novel tryptophan synthase beta-subunit from the hyperthermophile Thermotoga maritima. Quaternary structure, steady-state kinetics, and putative physiological role.Hettwer S, Sterner R2002 Mar 811756459