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2.6.1.109 |
Description |
8-amino-3,8-dideoxy-alpha-D-manno-octulosonate transaminase |
Alternative names |
kdnA (gene name) |
Catalyzed reaction |
8-amino-3,8-dideoxy-alpha-D-manno-octulosonate + 2-oxoglutarate <=> 8-dehydro-3-deoxy-alpha-D-manno-octulosonate + L-glutamate |
Cofactor |
Pyridoxal-phosphate. |
Comments |
The enzyme, characterized from the bacterium Shewanella oneidensis, forms 8-amino-3,8-dideoxy-alpha-D-manno-octulosonate, an aminated form of Kdo found in lipopolysaccharides of members of the Shewanella genus. |
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Lipopolysaccharide (LPS) is composed of a hydrophobic anchor, known as lipid A, an inner core oligosaccharide, and a repeating O-antigen polysaccharide. In nearly all species, the first sugar bridging the hydrophobic lipid A and the polysaccharide domain is 3-deoxy-d-manno-octulosonic acid (Kdo), and thus it is critically important for LPS biosynthesis. Modifications to lipid A have been shown to be important for resistance to antimicrobial peptides as well as modulating recognition by the mammalian innate immune system. Therefore, lipid A derivatives have been used for development of vaccine strains and vaccine adjuvants. One derivative that has yet to be studied is 8-amino-3,8-dideoxy-d-manno-octulosonic acid (Kdo8N), which is found exclusively in marine bacteria of the genus Shewanella. Expression of these genes recombinantly in Escherichia coli resulted in lipid A containing Kdo8N, and in vitro assays confirmed their proposed enzymatic function. |
PDB |
5K8B; |
Organisms |
-Eubacteria |
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Family |
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Links |
Enzyme (activities) 2.6.1.109
BRENDA (activities) 2.6.1.109
KEGG (pathways) 2.6.1.109
PLPMDB (PLP mutants) 2.6.1.109
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References |
Articles on 2.6.1.109 |
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last changed |
2017/09/06 11:31 |
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