EC number:4.2.1.118

Enzyme

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EC Tree
     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.1 Hydro-lyases
ID:4.2.1.118
Description:3-dehydroshikimate dehydratase.
Cath: 3.20.20.150;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.1.118
BRENDA Enzyme Link: BRENDA 4.2.1.118
KEGG Enzyme Link: KEGG4.2.1.118
BioCyc Enzyme Link: BioCyc 4.2.1.118
ExPASy Enzyme Link: ExPASy4.2.1.118
EC2PDB Enzyme Link: EC2PDB 4.2.1.118
ExplorEnz Enzyme Link: ExplorEnz 4.2.1.118
PRIAM enzyme-specific profiles Link: PRIAM 4.2.1.118
IntEnz Enzyme Link: IntEnz 4.2.1.118
MEDLINE Enzyme Link: MEDLINE 4.2.1.118

EC number:4.2.1.118

MSA:

4.2.1.118;
Phylogenetic Tree:

4.2.1.118;
Uniprot:
M-CSA:
RHEA:24848 3-dehydroshikimate = 3,4-dihydroxybenzoate + H2O
RULE(radius=1) [*:1]-[CH;+0:2]1-[CH2;+0:3]-[C;H0;+0:4](-[*:5])=[CH;+0:6]-[C;H0;+0:7](=[O;H0;+0:8])-[CH;+0:9]-1-[*:10]>>[*:1]-[c;H0;+0:2]1:[cH;+0:3]:[c;H0;+0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[c;H0;+0:9]:1-[*:10].[OH2;+0:8]
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References

TitleAuthorsDatePubMed ID
Unusual ancestry of dehydratases associated with quinate catabolism in Acinetobacter calcoaceticus.Elsemore DA, Ornston LN1995 Oct7592351
The missing link in petrobactin biosynthesis: asbF encodes a (-)-3-dehydroshikimate dehydratase.Fox DT, Hotta K, Kim CY, Koppisch AT2008 Nov 2518975921
Structural and functional analysis of AsbF: origin of the stealth 3,4-dihydroxybenzoic acid subunit for petrobactin biosynthesis.Pfleger BF, Kim Y, Nusca TD, Maltseva N, Lee JY, Rath CM, Scaglione JB, Janes BK, Anderson EC, Bergman NH, Hanna PC, Joachimiak A, Sherman DH2008 Nov 418955706