EC number:3.5.1.88
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.1 In linear amides |
| ID: | 3.5.1.88 |
|---|---|
| Description: | Peptide deformylase. |
| Alternative Name: |
Polypeptide deformylase. PDF. |
| Cath: | 3.90.45.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.1.88 |
| BRENDA Enzyme Link: | BRENDA 3.5.1.88 |
| KEGG Enzyme Link: | KEGG3.5.1.88 |
| BioCyc Enzyme Link: | BioCyc 3.5.1.88 |
| ExPASy Enzyme Link: | ExPASy3.5.1.88 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.1.88 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.1.88 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.1.88 |
| IntEnz Enzyme Link: | IntEnz 3.5.1.88 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.1.88 |
| RHEA:24420 | H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-terminal L-methionyl-[peptide] |
| RULE(radius=1) | [*:1]-[NH;+0:2]-[CH;+0:3]=[*:4].[OH2;+0:5]>>[*:1]-[NH2;+0:2].[*:4]=[CH;+0:3]-[OH;+0:5] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Structure of peptide deformylase and identification of the substrate binding site. | Becker A, Schlichting I, Kabsch W, Schultz S, Wagner AF | 1998 May 8 | 9565550 |
| Crystal structure of the Escherichia coli peptide deformylase. | Chan MK, Gong W, Rajagopalan PT, Hao B, Tsai CM, Pei D | 1997 Nov 11 | 9374869 |
| Fluid replacement with special reference to burned patients. | Bhantooa Dhurmadut | 1977 Mar 10 | 846875 |
| Zinc is the metal cofactor of Borrelia burgdorferi peptide deformylase. | Nguyen KT, Wu JC, Boylan JA, Gherardini FC, Pei D | 2007 Dec 15 | 17977509 |