UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase | |||||||||
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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 UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + L-glutamate
This enzyme is a pyridoxal-phosphate protein.
References
- ↑ Schoenhofen, I.C.; McNally, D.J.; Vinogradov, E.; Whitfield, D.; Young, N.M.; Dick, S.; Wakarchuk, W.W.; Brisson, J.R.; Logan, S.M. (2006). "Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways". J. Biol. Chem. 281: 723–732. doi:10.1074/jbc.m511021200. PMID 16286454.
- ↑ Schoenhofen, I.C.; Lunin, V.V.; Julien, J.P.; Li, Y.; Ajamian, E.; Matte, A.; Cygler, M.; Brisson, J.R.; Aubry, A.; Logan, S.M.; Bhatia, S.; Wakarchuk, W.W.; Young, N.M. (2006). "Structural and functional characterization of PseC, an aminotransferase involved in the biosynthesis of pseudaminic acid, an essential flagellar modification in Helicobacter pylori". J. Biol. Chem. 281: 8907–8916. 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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