| ID: | 4.1.1.90 |
|---|---|
| Description: | Peptidyl-glutamate 4-carboxylase. |
| Alternative Name: |
Vitamin K-dependent carboxylase. Gamma-glutamyl carboxylase. |
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 4.1.1.90 |
| BRENDA Enzyme Link: | BRENDA 4.1.1.90 |
| KEGG Enzyme Link: | KEGG4.1.1.90 |
| BioCyc Enzyme Link: | BioCyc 4.1.1.90 |
| ExPASy Enzyme Link: | ExPASy4.1.1.90 |
| EC2PDB Enzyme Link: | EC2PDB 4.1.1.90 |
| ExplorEnz Enzyme Link: | ExplorEnz 4.1.1.90 |
| PRIAM enzyme-specific profiles Link: | PRIAM 4.1.1.90 |
| IntEnz Enzyme Link: | IntEnz 4.1.1.90 |
| MEDLINE Enzyme Link: | MEDLINE 4.1.1.90 |
| RHEA:45140 | 2,3-epoxyphylloquinone + 4-carboxy-L-glutamyl-[protein] + H(+) + H2O = CO2 + L-glutamyl-[protein] + O2 + phylloquinol |
| RULE(radius=1) | [*:1]-[C;H0;+0:2]12-[O;H0;+0:3]-[C;H0;+0:4]-1(-[*:5])-[C;H0;+0:6](=[O;H0;+0:7])-[*:8]:[*:9]-[C;H0;+0:10]-2=[O;H0;+0:11].[*:12]-[CH;+0:13](-[*:14])-[C;H0;+0:15](=[*:16])-[OH;+0:17].[H+;H0:18].[OH2;+0:19]>>[*:12]-[CH2;+0:13]-[*:14].[*:1]-[c;H0;+0:2]1:[c;H0;+0:4](-[*:5]):[c;H0;+0:6](-[OH;+0:7]):[*:8]:[*:9]:[c;H0;+0:10]:1-[OH;+0:11].[*:16]=[C;H0;+0:15]=[O;H0;+0:17].[O;H0;+0:3]=[O;H0;+0:19] |
| Reaction | ![]() |
| Core-to-Core |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The stereochemistry of hydrogen abstraction in vitamin K-dependent carboxylation. | Decottignies-Le Maréchal P, Ducrocq C, Marquet A, Azerad R | 1984 Dec 25 | 6150930 |
| Reaction mechanism of the vitamin K-dependent glutamate carboxylase: a computational study. | Silva PJ, Ramos MJ | 2007 Nov 8 | 17935315 |
| Brønsted analysis reveals Lys218 as the carboxylase active site base that deprotonates vitamin K hydroquinone to initiate vitamin K-dependent protein carboxylation. | Rishavy MA, Hallgren KW, Yakubenko AV, Shtofman RL, Runge KW, Berkner KL | 2006 Nov 7 | 17073445 |