Enzyme

Download
EC Tree
     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.1 Hydro-lyases
ID:4.2.1.10
Description:3-dehydroquinate dehydratase.
Prosite: PDOC00789; PDOC00788;
PDB:
PDBScop
1GQO 8029876; 8042255; 8029876; 8042255; 8029876; 8042255; 8029876; 8042255; 8029876; 8042255; 8029876; 8042255; 8029876; 8042255; 8029876; 8042255; 8029876; 8042255; 8029876; 8042255; 8029876; 8042255; 8029876; 8042255; 8029876; 8042255; 8029876; 8042255; 8029876; 8042255; 8029876; 8042255; 8029876; 8042255; 8029876; 8042255; 8029876; 8042255; 8029876; 8042255; 8029876; 8042255; 8029876; 8042255; 8029876; 8042255; 8029876; 8042255;
1UQR 8029590; 8041969; 8029590; 8041969; 8029590; 8041969; 8029590; 8041969; 8029590; 8041969; 8029590; 8041969; 8029590; 8041969; 8029590; 8041969; 8029590; 8041969; 8029590; 8041969; 8029590; 8041969; 8029590; 8041969;
2WKS 8026978; 8039357; 8026978; 8039357; 8026978; 8039357; 8026978; 8039357; 8026978; 8039357; 8026978; 8039357;
4B6S 8026978; 8039357; 8026978; 8039357; 8026978; 8039357;
4B6R 8026978; 8039357; 8026978; 8039357; 8026978; 8039357;
 » show all

Cath: 1.20.1090.10; 1.20.1280.250; 3.20.20.70; 3.40.50.720; 3.40.50.9100; 3.40.50.10860; 3.40.50.1970;

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.1.10
BRENDA Enzyme Link: BRENDA 4.2.1.10
KEGG Enzyme Link: KEGG4.2.1.10
BioCyc Enzyme Link: BioCyc 4.2.1.10
ExPASy Enzyme Link: ExPASy4.2.1.10
EC2PDB Enzyme Link: EC2PDB 4.2.1.10
ExplorEnz Enzyme Link: ExplorEnz 4.2.1.10
PRIAM enzyme-specific profiles Link: PRIAM 4.2.1.10
IntEnz Enzyme Link: IntEnz 4.2.1.10
MEDLINE Enzyme Link: MEDLINE 4.2.1.10
MSA:

4.2.1.10;

Phylogenetic Tree:

4.2.1.10;

Uniprot:
M-CSA:
RHEA:21096 3-dehydroquinate = 3-dehydroshikimate + H2O
RULE(radius=1) [*:1]-[C;H0;+0:2](-[*:3])(-[OH;+0:4])-[CH2;+0:5]-[*:6]>>[*:1]-[C;H0;+0:2](-[*:3])=[CH;+0:5]-[*:6].[OH2;+0:4]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Identification of polyketide inhibitors targeting 3-dehydroquinate dehydratase in the shikimate pathway of Enterococcus faecalis.Cheung VW, Xue B, Hernandez-Valladares M, Go MK, Tung A, Aguda AH, Robinson RC, Yew WS201425072253
The purification and characterization of 3-dehydroquinase from Streptomyces coelicolor.White PJ, Young J, Hunter IS, Nimmo HG, Coggins JR1990 Feb 12306211
Insights into the mechanism of type I dehydroquinate dehydratases from structures of reaction intermediates.Light SH, Minasov G, Shuvalova L, Duban ME, Caffrey M, Anderson WF, Lavie A2011 Feb 421087925
Specificity of substrate recognition by type II dehydroquinases as revealed by binding of polyanions.Evans LD, Roszak AW, Noble LJ, Robinson DA, Chalk PA, Matthews JL, Coggins JR, Price NC, Lapthorn AJ2002 Oct 2312387860
The structure and mechanism of the type II dehydroquinase from Streptomyces coelicolor.Roszak AW, Robinson DA, Krell T, Hunter IS, Fredrickson M, Abell C, Coggins JR, Lapthorn AJ2002 Apr11937054
The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction.Gourley DG, Shrive AK, Polikarpov I, Krell T, Coggins JR, Hawkins AR, Isaacs NW, Sawyer L1999 Jun10360352