EC number:4.1.2.19
| ID: | 4.1.2.19 |
|---|---|
| Description: | Rhamnulose-1-phosphate aldolase. |
| Alternative Name: |
L-rhamnulose-phosphate aldolase. L-rhamnulose-1-phosphate lactaldehyde-lyase. L-rhamnulose 1-phosphate aldolase. |
| Cath: | 3.40.225.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 4.1.2.19 |
| BRENDA Enzyme Link: | BRENDA 4.1.2.19 |
| KEGG Enzyme Link: | KEGG4.1.2.19 |
| BioCyc Enzyme Link: | BioCyc 4.1.2.19 |
| ExPASy Enzyme Link: | ExPASy4.1.2.19 |
| EC2PDB Enzyme Link: | EC2PDB 4.1.2.19 |
| ExplorEnz Enzyme Link: | ExplorEnz 4.1.2.19 |
| PRIAM enzyme-specific profiles Link: | PRIAM 4.1.2.19 |
| IntEnz Enzyme Link: | IntEnz 4.1.2.19 |
| MEDLINE Enzyme Link: | MEDLINE 4.1.2.19 |
| RHEA:19689 | L-rhamnulose 1-phosphate = (S)-lactaldehyde + dihydroxyacetone phosphate |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[CH;+0:4](-[*:5])-[OH;+0:6]>>[*:1]-[CH2;+0:2]-[*:3].[*:5]-[CH;+0:4]=[O;H0;+0:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Antenna domain mobility and enzymatic reaction of L-rhamnulose-1-phosphate aldolase. | Grueninger D, Schulz GE | 2008 Jan 15 | 18085797 |
| Structure and catalytic mechanism of L-rhamnulose-1-phosphate aldolase. | Kroemer M, Merkel I, Schulz GE | 2003 Sep 16 | 12962479 |