EC number:2.6.1.98
| ID: | 2.6.1.98 |
|---|---|
| Description: | UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase. |
| Cath: | 3.30.360.10; 3.40.50.720; 3.40.640.10; 3.90.1150.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 2.6.1.98 |
| BRENDA Enzyme Link: | BRENDA 2.6.1.98 |
| KEGG Enzyme Link: | KEGG2.6.1.98 |
| BioCyc Enzyme Link: | BioCyc 2.6.1.98 |
| ExPASy Enzyme Link: | ExPASy2.6.1.98 |
| EC2PDB Enzyme Link: | EC2PDB 2.6.1.98 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.6.1.98 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.6.1.98 |
| IntEnz Enzyme Link: | IntEnz 2.6.1.98 |
| MEDLINE Enzyme Link: | MEDLINE 2.6.1.98 |
| RHEA:33583 | L-glutamate + UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate = 2-oxoglutarate + UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[CH;+0:6](-[*:7])-[NH2;+0:8]>>[*:5]-[C;H0;+0:6](-[*:7])=[O;H0;+0:4].[*:1]-[CH;+0:2](-[*:3])-[NH2;+0:8] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Structural and functional studies of WlbA: A dehydrogenase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid . | Thoden JB, Holden HM | 2010 Sep 14 | 20690587 |
| Structural analysis of WbpE from Pseudomonas aeruginosa PAO1: a nucleotide sugar aminotransferase involved in O-antigen assembly. | Larkin A, Olivier NB, Imperiali B | 2010 Aug 24 | 20604544 |
| Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: enzymes in the Wbp pathway responsible for O-antigen assembly in Pseudomonas aeruginosa PAO1. | Larkin A, Imperiali B | 2009 Jun 16 | 19348502 |
| Characterization of WbpB, WbpE, and WbpD and reconstitution of a pathway for the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid in Pseudomonas aeruginosa. | Westman EL, McNally DJ, Charchoglyan A, Brewer D, Field RA, Lam JS | 2009 May 1 | 19282284 |