EC number:2.7.1.60
Enzyme
Download| EC Tree |
| 2. Transferases |
| 2.7 Transferring phosphorus-containing groups |
| 2.7.1 Phosphotransferases with an alcohol group as acceptor |
| ID: | 2.7.1.60 |
|---|---|
| Description: | N-acylmannosamine kinase. |
| Cath: | 3.30.420.40; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 2.7.1.60 |
| BRENDA Enzyme Link: | BRENDA 2.7.1.60 |
| KEGG Enzyme Link: | KEGG2.7.1.60 |
| BioCyc Enzyme Link: | BioCyc 2.7.1.60 |
| ExPASy Enzyme Link: | ExPASy2.7.1.60 |
| EC2PDB Enzyme Link: | EC2PDB 2.7.1.60 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.7.1.60 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.7.1.60 |
| IntEnz Enzyme Link: | IntEnz 2.7.1.60 |
| MEDLINE Enzyme Link: | MEDLINE 2.7.1.60 |
| RHEA:25253 | ATP + N-acetyl-D-mannosamine = ADP + H(+) + N-acetyl-D-mannosamine 6-phosphate |
| RULE(radius=1) | [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Identifying latent enzyme activities: substrate ambiguity within modern bacterial sugar kinases. | Miller BG, Raines RT | 2004 Jun 1 | 15157072 |
| RHEA:23832 | an N-acyl-D-mannosamine + ATP = ADP + an N-acyl-D-mannosamine 6-phosphate + H(+) |
| RULE(radius=1) | [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. Purification and characterization of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase. | Hinderlich S, Stäsche R, Zeitler R, Reutter W | 1997 Sep 26 | 9305887 |
| Divergent evolution of function in the ROK sugar kinase superfamily: role of enzyme loops in substrate specificity. | Larion M, Moore LB, Thompson SM, Miller BG | 2007 Nov 27 | 17979299 |
| Identifying latent enzyme activities: substrate ambiguity within modern bacterial sugar kinases. | Miller BG, Raines RT | 2004 Jun 1 | 15157072 |