Enzyme

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EC Tree
     4. Lyases
        4.1 Carbon-carbon lyases
            4.1.3 Oxo-acid-lyases
ID:4.1.3.6
Description:Citrate (pro-3S)-lyase.
Alternative Name: Citritase.
Citridesmolase.
Citrate lyase.
Citrate aldolase.
Citratase.
Citrase.
Cath: 1.10.287.2470; 3.20.20.60; 3.40.1080.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.1.3.6
BRENDA Enzyme Link: BRENDA 4.1.3.6
KEGG Enzyme Link: KEGG4.1.3.6
BioCyc Enzyme Link: BioCyc 4.1.3.6
ExPASy Enzyme Link: ExPASy4.1.3.6
EC2PDB Enzyme Link: EC2PDB 4.1.3.6
ExplorEnz Enzyme Link: ExplorEnz 4.1.3.6
PRIAM enzyme-specific profiles Link: PRIAM 4.1.3.6
IntEnz Enzyme Link: IntEnz 4.1.3.6
MEDLINE Enzyme Link: MEDLINE 4.1.3.6
MSA:

4.1.3.6;

Phylogenetic Tree:

4.1.3.6;

Uniprot:
M-CSA:
RHEA:10760 citrate = acetate + oxaloacetate
RULE(radius=1) [*:1]-[C;H0;+0:2](-[*:3])(-[OH;+0:4])-[CH2;+0:5]-[*:6]>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:6]-[CH3;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Purification and properties of citrate lyase from Escherichia coli.Nilekani S, SivaRaman C1983 Sep 276354265
Characterization of the isolated transferase subunit of citrate lyase as a CoA-Transferase. Evidence against a covalent enzyme-substrate intermediate.Dimroth P, Loyal R, Eggerer H1977 Nov 1336371
Citridesmolase: its properties and mode of action.DAGLEY S, DAWES EA1955 Jun13239657