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

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Short description: Class of enzymes
UDP-N-acetylglucosamine 4,6-dehydratase (configuration-inverting)
Identifiers
EC number4.2.1.115
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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 [math]\displaystyle{ \rightleftharpoons }[/math] UDP-2-acetamido-2,6-dideoxy-β-L-arabino-hex-4-ulose + H2O

This enzyme contains NADP+ as a cofactor.

References

  1. "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. August 2006. doi:10.1074/jbc.m602393200. PMID 16651261. 
  2. "Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori". Molecular Microbiology 48 (6): 1579–92. June 2003. doi:10.1046/j.1365-2958.2003.03527.x. PMID 12791140. 
  3. "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. September 2006. doi:10.1093/glycob/cwl010. PMID 16751642. 

External links