EC number:4.2.1.117

Enzyme

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EC Tree
     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.1 Hydro-lyases
ID:4.2.1.117
Description:2-methylcitrate dehydratase (2-methyl-trans-aconitate forming).

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.1.117
BRENDA Enzyme Link: BRENDA 4.2.1.117
KEGG Enzyme Link: KEGG4.2.1.117
BioCyc Enzyme Link: BioCyc 4.2.1.117
ExPASy Enzyme Link: ExPASy4.2.1.117
EC2PDB Enzyme Link: EC2PDB 4.2.1.117
ExplorEnz Enzyme Link: ExplorEnz 4.2.1.117
PRIAM enzyme-specific profiles Link: PRIAM 4.2.1.117
IntEnz Enzyme Link: IntEnz 4.2.1.117
MEDLINE Enzyme Link: MEDLINE 4.2.1.117

EC number:4.2.1.117

MSA:

4.2.1.117;
Phylogenetic Tree:

4.2.1.117;
Uniprot:
M-CSA:
RHEA:26522 (2S,3S)-2-methylcitrate = 2-methyl-trans-aconitate + H2O
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[C;H0;+0:4](-[*:5])(-[*:6])-[OH;+0:7]>>[*:1]-[C;H0;+0:2](-[*:3])=[C;H0;+0:4](-[*:5])-[*:6].[OH2;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The acnD genes of Shewenella oneidensis and Vibrio cholerae encode a new Fe/S-dependent 2-methylcitrate dehydratase enzyme that requires prpF function in vivo.Grimek TL, Escalante-Semerena JC2004 Jan14702315