| Entry |
|
| Name |
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose transaminase;
TylB;
TDP-3-keto-6-deoxy-D-glucose 3-aminotransferase;
TDP-3-dehydro-6-deoxy-D-glucose 3-aminotransferase;
dTDP-3-keto-6-deoxy-D-glucose 3-aminotransferase;
dTDP-3-dehydro-6-deoxy-D-glucose 3-aminotransferase
|
| Class |
Transferases;
Transferring nitrogenous groups;
Transaminases
 |
| Sysname |
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose:2-oxoglutarate aminotransferase
|
| Reaction(IUBMB) |
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose + 2-oxoglutarate = dTDP-3-dehydro-6-deoxy-alpha-D-glucopyranose + L-glutamate [RN: R06423]
|
| Reaction(KEGG) |
|
| Substrate |
dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose;
2-oxoglutarate [CPD: C00026]
|
| Product |
dTDP-3-dehydro-6-deoxy-alpha-D-glucopyranose [CPD: C11908];
L-glutamate [CPD: C00025]
|
| Comment |
A pyridoxal-phosphate protein. The reaction occurs in the reverse direction. The enzyme is involved in biosynthesis of D-mycaminose.
|
| Reference |
|
| Authors |
Melancon CE 3rd, Hong L, White JA, Liu YN, Liu HW |
| Title |
Characterization of TDP-4-keto-6-deoxy-D-glucose-3,4-ketoisomerase from the D-mycaminose biosynthetic pathway of Streptomyces fradiae: in vitro activity and substrate specificity studies. |
| Journal |
Biochemistry. 46 (2007) 577-90. |
| Organism |
Streptomyces fradiae |
| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: |