UDP-N-acetylglucosamine 4,6-dehydratase (configuration-inverting)

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UDP-N-acetylglucosamine 4,6-dehydratase (configuration-inverting)
Identifiers
EC no.4.2.1.115
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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UDP-N-acetylglucosamine 4,6-dehydratase (configuration-inverting) (EC 4.2.1.115, FlaA1, UDP-N-acetylglucosamine 5-inverting 4,6-dehydratase, PseB, UDP-N-acetylglucosamine hydro-lyase (inverting, UDP-2-acetamido-2,6-dideoxy-β-L)arabino-hex-4-ulose-forming)) is an enzyme with systematic name UDP-N-acetyl-α-D-glucosamine hydro-lyase (inverting; UDP-2-acetamido-2,6-dideoxy-β-L-arabino-hex-4-ulose-forming).[1][2][3] This enzyme catalyses the following chemical reaction

UDP-N-acetyl-α-D-glucosamine UDP-2-acetamido-2,6-dideoxy-β-L-arabino-hex-4-ulose + H2O

This enzyme contains NADP+ as a cofactor.

References[edit]

  1. ^ Ishiyama N, Creuzenet C, Miller WL, Demendi M, Anderson EM, Harauz G, Lam JS, Berghuis AM (August 2006). "Structural studies of FlaA1 from Helicobacter pylori reveal the mechanism for inverting 4,6-dehydratase activity". The Journal of Biological Chemistry. 281 (34): 24489–95. doi:10.1074/jbc.m602393200. PMID 16651261.
  2. ^ Schirm M, Soo EC, Aubry AJ, Austin J, Thibault P, Logan SM (June 2003). "Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori". Molecular Microbiology. 48 (6): 1579–92. doi:10.1046/j.1365-2958.2003.03527.x. PMID 12791140.
  3. ^ Schoenhofen IC, McNally DJ, Brisson JR, Logan SM (September 2006). "Elucidation of the CMP-pseudaminic acid pathway in Helicobacter pylori: synthesis from UDP-N-acetylglucosamine by a single enzymatic reaction". Glycobiology. 16 (9): 8C–14C. doi:10.1093/glycob/cwl010. PMID 16751642.

External links[edit]