| 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; |
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.| 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 |
| 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 |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Purification and properties of citrate lyase from Escherichia coli. | Nilekani S, SivaRaman C | 1983 Sep 27 | 6354265 |
| 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 H | 1977 Nov 1 | 336371 |
| Citridesmolase: its properties and mode of action. | DAGLEY S, DAWES EA | 1955 Jun | 13239657 |