Biology:UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase
From HandWiki
| UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 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 | ||||||||
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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 + 2-oxoglutarate [math]\displaystyle{ \rightleftharpoons }[/math] UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + L-glutamate
This enzyme is a pyridoxal-phosphate protein.
References
- ↑ "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. January 2006. doi:10.1074/jbc.m511021200. PMID 16286454.
- ↑ "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. March 2006. doi:10.1074/jbc.m512987200. PMID 16421095.
External links
- UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine+transaminase at the US National Library of Medicine Medical Subject Headings (MeSH)
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