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2.6.1.89 |
Activity |
2.6.1.89 |
Description |
dTDP-3-dehydro-6-deoxy-D-glucose aminotransferase |
Notes |
Only one functionally validated gene product (from T. thermosaccharolyticum). These bacterial enzymes are phylogenetically related to (and very difficult to distinguish from ) a number of other NDP-hexose aminotransferases, in particular those in family 2.6.1.106. |
PDB |
3FRK; |
PLP Fold Type |
I |
PLP-dependent Domain |
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Number of sequences |
5 |
Sequences in seed alignment |
|
Reference sequence |
AAR85519 |
Domain interval |
13-362 |
Catalytic site |
186 K |
| |
References |
Thoden JB, Schäffer C, Messner P, Holden HM. (2009) Structural Analysis of QdtB, an Aminotransferase Required for the Biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-d-glucose Biochemistry 48 1553–1561. Westman EL, McNally DJ, Charchoglyan A, Brewer D, Field RA, Lam JS. (2009) 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 J Biol Chem 284 11854-62. Pföstl A, Zayni S, Hofinger A, Kosma P, Schäffer C, Messner P. (2008) Biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-D-glucose Biochem J 410 187-94. Melançon CE 3rd, Hong L, White JA, Liu YN, Liu HW. (2007) 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 Biochemistry 46 577-90. Articles on 2.6.1.89 |
last changed |
2017/09/08 09:21 |
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