EC number:2.4.1.131
| ID: | 2.4.1.131 |
|---|---|
| Description: | GDP-Man:Man(3)GlcNAc(2)-PP-dolichol alpha-1,2-mannosyltransferase. |
3D structure
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.References
External Links
| UniProtKB Enzyme Link: | UniProtKB 2.4.1.131 |
| BRENDA Enzyme Link: | BRENDA 2.4.1.131 |
| KEGG Enzyme Link: | KEGG2.4.1.131 |
| BioCyc Enzyme Link: | BioCyc 2.4.1.131 |
| ExPASy Enzyme Link: | ExPASy2.4.1.131 |
| EC2PDB Enzyme Link: | EC2PDB 2.4.1.131 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.4.1.131 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.4.1.131 |
| IntEnz Enzyme Link: | IntEnz 2.4.1.131 |
| MEDLINE Enzyme Link: | MEDLINE 2.4.1.131 |
EC number:2.4.1.131
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:29523 | alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP-alpha-D-mannose = alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP + 2 H(+) |
| RULE(radius=1) | [*:1]-[O;H0;+0:2]-[CH;+0:3](-[*:4])-[*:5].[*:6]-[O;H0;+0:7]-[CH;+0:8](-[*:9])-[*:10]-[OH;+0:11].[*:12]-[OH;+0:13]>>[*:4]-[CH;+0:3](-[*:5])-[O;H0;+0:11]-[*:10]-[CH;+0:8](-[*:9])-[O;H0;+0:13]-[*:12].[*:1]-[OH;+0:2].[*:6]-[OH;+0:7] |
| Reaction |  |
| Core-to-Core | |
| Core-to-Core | |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The biosynthesis of oligosaccharide-lipids. Formation of an alpha-1,2-mannosyl-mannose linkage. | Schutzbach JS, Springfield JD, Jensen JW | 1980 May 10 | 6154707 |
| A severe human metabolic disease caused by deficiency of the endoplasmatic mannosyltransferase hALG11 leads to congenital disorder of glycosylation-Ip. | Rind N, Schmeiser V, Thiel C, Absmanner B, Lübbehusen J, Hocks J, Apeshiotis N, Wilichowski E, Lehle L, Körner C | 2010 Apr 15 | 20080937 |
| Biochemical characterization, membrane association and identification of amino acids essential for the function of Alg11 from Saccharomyces cerevisiae, an alpha1,2-mannosyltransferase catalysing two sequential glycosylation steps in the formation of the lipid-linked core oligosaccharide. | Absmanner B, Schmeiser V, Kämpf M, Lehle L | 2010 Feb 9 | 19929855 |
| LEW3, encoding a putative alpha-1,2-mannosyltransferase (ALG11) in N-linked glycoprotein, plays vital roles in cell-wall biosynthesis and the abiotic stress response in Arabidopsis thaliana. | Zhang M, Henquet M, Chen Z, Zhang H, Zhang Y, Ren X, van der Krol S, Gonneau M, Bosch D, Gong Z | 2009 Dec | 19732381 |
| In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis. | O'Reilly MK, Zhang G, Imperiali B | 2006 Aug 8 | 16878994 |