EC Number |
General Information |
Reference |
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2.7.8.36 | metabolism |
the enzyme is part of the broad-spectrum O-linked glycosylation pathway expressed by neisserial species, overview. PglB, -C, and -D are required for the synthesis of UDP-N'-diacetylbacillosamine (UDP-diNAcBac) and transfer of the phospho-diNAcBac to undecaprenyl phosphate. This glycoform can be further modified by the glycosyltransferases PglA and PglH/PglH2. The PglE glycosyltransferase can modify only the disaccharide glycoform generated by PglA |
-, 736369 |
2.7.8.36 | physiological function |
a conserved proline residue in the reentrant membrane-helix drives polyprenol phosphate recognition and specificity. Polyprenol phosphates at physiologically relevant levels increase the disorder of the local lipid bilayer, this effect is confined to polyprenol phosphates with specific isoprene geometries |
-, 760438 |
2.7.8.36 | physiological function |
the PglD and PglC proteins carry out NAD+-dependent dehydratase and aminotransferase reactions, respectively, to convert UDP-GlcNAc to UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha--D-glucose. PglB then acts as a bifunctional enzyme, which catalyzes the amino acetylation of UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-glucose to form UDP-di-N-acetylbacillosamine (diNAcBac) and the transfer of the phospho-sugar to undecaprenyl phosphate |
-, 736369 |
2.7.8.36 | physiological function |
the PglD and PglC proteins carry out NAD+-dependent dehydratase and aminotransferase reactions, respectively, to convert UDP-GlcNAc to UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-glucose. PglB then acts as a bifunctional enzyme, which catalyzes the amino acetylation of UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-glucose to form UDP-di-N-acetylbacillosamine (diNAcBac) and the transfer of the phospho-sugar to undecaprenyl phosphate |
-, 736369 |