A pyridoxal 5'-phosphate protein. The enzyme transfers the primary amino group of L-glutamate to C-4'' of UDP-4-dehydro sugars, forming a C-N bond in a stereo configuration opposite to that of UDP. The enzyme from the bacterium Bacillus cereus has been shown to act on UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose, UDP-beta-L-threo-pentapyranos-4-ulose, UDP-4-dehydro-6-deoxy-D-glucose, and UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose. cf. EC 2.6.1.34, UDP-N-acetylbacillosamine transaminase, which catalyses a similar reaction, but forms the C-N bond in the same stereo configuration as that of UDP.
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
A pyridoxal 5'-phosphate protein. The enzyme transfers the primary amino group of L-glutamate to C-4'' of UDP-4-dehydro sugars, forming a C-N bond in a stereo configuration opposite to that of UDP. The enzyme from the bacterium Bacillus cereus has been shown to act on UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose, UDP-beta-L-threo-pentapyranos-4-ulose, UDP-4-dehydro-6-deoxy-D-glucose, and UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose. cf. EC 2.6.1.34, UDP-N-acetylbacillosamine transaminase, which catalyses a similar reaction, but forms the C-N bond in the same stereo configuration as that of UDP.
the enzyme is involved biosynthesis of pseudaminic acid. Helicobacter pylori flagellin is heavily glycosylated with pseudaminic acid. The glycosylation process is essential for assembly of functional flagellar filaments and consequent bacterial motility. Motility is a key virulence factor for this and other important pathogens
the enzyme is involved biosynthesis of pseudaminic acid. Helicobacter pylori flagellin is heavily glycosylated with pseudaminic acid. The glycosylation process is essential for assembly of functional flagellar filaments and consequent bacterial motility. Motility is a key virulence factor for this and other important pathogens
the enzyme is involved biosynthesis of 5,7-bis(acetylamino)-3,5,7,9-tetradeoxy-L-glycero-alpha-L-manno-2-nonulopyranosonic acid (pseudaminic acid). Helicobacter pylori flagellin is heavily glycosylated with pseudaminic acid. The glycosylation process is essential for assembly of functional flagellar filaments and consequent bacterial motility. Motility is a key virulence factor for this and other important pathogens
PseC is a homodimer in solution (as shown by dynamic light scattering) as well as in the crystal structure, where the two monomers are related by 2fold crystallographic symmetry. The inter-subunit interactions are extensive, involving several elements of secondary structure, predominantly from the N-terminal domains of both monomers. Each monomer contributes to the active site
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the native protein, its complexes with pyridoxal 5'-phosphate alone and in combination with UDP-4-amino-4,6-dideoxy-L-N-acetyl-beta-L-altrosamine. A crystal of apo-PseC is obtained in 2 days at 20°C from a hanging drop by mixing 0.0015 ml of protein in buffer with 0.0015 ml of reservoir solution containing 0.2 M ammonium acetate, 0.1 M trisodium citrate, pH 5.6, 30% polyethylene glycol 4000. The crystals belong to space group P2(1)2(1)2 with unit cell dimensions a = 87.7, b = 155.4, and c = 71.5 A and Z = 4
the enzyme is involved biosynthesis of 5,7-bis(acetylamino)-3,5,7,9-tetradeoxy-L-glycero-alpha-L-manno-2-nonulopyranosonic acid (pseudaminic acid). Helicobacter pylori flagellin is heavily glycosylated with pseudaminic acid. The glycosylation process is essential for assembly of functional flagellar filaments and consequent bacterial motility. Because motility is a key virulence factor for this and other important pathogens, the pseudaminic acid biosynthetic pathway offers potential for novel therapeutic targets
Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways
Structural and functional characterization of PseC, an aminotransferase involved in the biosynthesis of pseudaminic acid, an essential flagellar modification in Helicobacter pylori