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UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine transaminase
| Field | Value |
|---|---|
| Name | UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine transaminase |
| EC_number | 2.6.1.91 |
UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine transaminase (, pglE (gene)) is an enzyme with systematic name UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine:2-oxoglutarate aminotransferase. This enzyme catalyses the following chemical reaction
: UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine + 2-oxoglutarate \rightleftharpoons UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose + L-glutamate
This enzyme is a pyridoxal-phosphate protein.
References
References
- (November 2006). "In vitro biosynthesis of UDP-N,N'-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system". Biochemistry.
- (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.
- (February 2008). "Structure and active site residues of PglD, an N-acetyltransferase from the bacillosamine synthetic pathway required for N-glycan synthesis in Campylobacter jejuni". Biochemistry.
- (June 2011). "Biochemical characterization of the O-linked glycosylation pathway in Neisseria gonorrhoeae responsible for biosynthesis of protein glycans containing N,N'-diacetylbacillosamine". Biochemistry.
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