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PUMA2 -- Evolutionary Analysis of Metabolism | |
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PUMA2 is not being maintained or updated by Argonne National Laboratory and will be taken down in the near future. If there is any data here that you wish to preserve, you are responsible for downloading it. An overview of the bioinformatics research being conducted at the Mathematics and Computer Science Division is available at this page. |
| EC-number: 3.4.16.6 ----- carboxypeptidase D |
| EC-NUMBER | 3.4.16.6 | |
| ENZYME-NAME | carboxypeptidase D | |
| ENZYME-SYSNAME | A carboxypeptidase with optimum pH 4.5-6.0, inhibited by diisopropyl fluorophosphate, and sensitive to thiol-blocking reagents (reviewed in [1]). In peptidase family S10 (carboxypeptidase C family). Formerly EC 3.4.12.1 and EC 3.4.21.13, and EC 3.4.16.1 | |
| ENZYME-CLASS | Hydrolases Acting on peptide bonds (peptidases) Serine-type carboxypeptidases | |
| SYNONYMS | CPDW-II; KEX1 carboxypeptidase;; KEX1 proteinase;; KEX1DELTAp;; >>more synonyms | |
| REACTION | Preferential release of a C-terminal arginine or lysine residueINHIBITOR Isoflurophate [CPD:C00202] | Thiol-blocking reagent [CPD:C00648] |
| PATHWAY | EMP-PATHWAYS: NO EMP PATHWAY FOUND | |
| KEGG-PATHWAYS: NO KEGG PATHWAY FOUND | ||
| GO_TERM | GO:0004187:carboxypeptidase D activity | |
| ENZYME-COMMENT | NULL | |
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To perform phylogenetic analysis:
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