UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase (EC 2.6.1.92, PseC) is an enzyme with systematic name UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine:2-oxoglutarate aminotransferase.[1][2] This enzyme catalyses the following chemical reaction
| UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.92 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine + 2-oxoglutarate UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + L-glutamate
This enzyme is a pyridoxal-phosphate protein.
References
edit- ^ Schoenhofen IC, McNally DJ, Vinogradov E, Whitfield D, Young NM, Dick S, Wakarchuk WW, Brisson JR, Logan SM (January 2006). "Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways". The Journal of Biological Chemistry. 281 (2): 723–32. doi:10.1074/jbc.m511021200. PMID 16286454.
- ^ Schoenhofen IC, Lunin VV, Julien JP, Li Y, Ajamian E, Matte A, Cygler M, Brisson JR, Aubry A, Logan SM, Bhatia S, Wakarchuk WW, Young NM (March 2006). "Structural and functional characterization of PseC, an aminotransferase involved in the biosynthesis of pseudaminic acid, an essential flagellar modification in Helicobacter pylori". The Journal of Biological Chemistry. 281 (13): 8907–16. doi:10.1074/jbc.m512987200. PMID 16421095.
External links
edit- UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine+transaminase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
