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

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

UDP-N-acetylglucosamine 4,6-dehydratase (configuration-retaining) (EC 4.2.1.135 [17] , PglF) is an enzyme with systematic name UDP-N-acetyl-alpha-D-glucosamine hydro-lyase (configuration-retaining; UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose-forming).[1][2] This enzyme catalyses the following chemical reaction

UDP-N-acetyl-alpha-D-glucosamineUDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose + H2O

This enzyme contains NAD+ as a cofactor.

UDP-N-acetylglucosamine 4,6-dehydratase (configuration-retaining)
Identifiers
EC number4.2.1.135 [4]
Databases
IntEnzIntEnz view [5]
BRENDABRENDA entry [6]
ExPASyNiceZyme view [7]
KEGGKEGG entry [8]
MetaCycmetabolic pathway [9]
PRIAMprofile [10]
PDB structuresRCSB PDB [11] PDBe [12] PDBsum [13]
Search
PMCarticles [14]
PubMedarticles [15]
NCBIproteins [16]

References

[1]
Citation Link//www.ncbi.nlm.nih.gov/pubmed/16286454Schoenhofen IC, McNally DJ, Vinogradov E, Whitfield D, Young NM, Dick S, Wakarchuk WW, Brisson JR, Logan SM (January 2006). "Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways". The Journal of Biological Chemistry. 281 (2): 723–32. doi:10.1074/jbc.m511021200. PMID 16286454.
Sep 29, 2019, 1:58 PM
[2]
Citation Link//www.ncbi.nlm.nih.gov/pubmed/17087520Olivier NB, Chen MM, Behr JR, Imperiali B (November 2006). "In vitro biosynthesis of UDP-N,N'-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system". Biochemistry. 45 (45): 13659–69. doi:10.1021/bi061456h. PMC 2542654. PMID 17087520.
Sep 29, 2019, 1:58 PM
[3]
Citation Linkmeshb.nlm.nih.govUDP-N-acetylglucosamine+4,6-dehydratase+(configuration-retaining)
Sep 29, 2019, 1:58 PM
[4]
Citation Linkwww.qmul.ac.uk4.2.1.135
Sep 29, 2019, 1:58 PM
[5]
Citation Linkwww.ebi.ac.ukIntEnz view
Sep 29, 2019, 1:58 PM
[6]
Citation Linkwww.brenda-enzymes.orgBRENDA entry
Sep 29, 2019, 1:58 PM
[7]
Citation Linkwww.expasy.orgNiceZyme view
Sep 29, 2019, 1:58 PM
[8]
Citation Linkwww.genome.jpKEGG entry
Sep 29, 2019, 1:58 PM
[9]
Citation Linkbiocyc.orgmetabolic pathway
Sep 29, 2019, 1:58 PM
[10]
Citation Linkpriam.prabi.frprofile
Sep 29, 2019, 1:58 PM
[11]
Citation Linkwww.rcsb.orgRCSB PDB
Sep 29, 2019, 1:58 PM
[12]
Citation Linkwww.ebi.ac.ukPDBe
Sep 29, 2019, 1:58 PM
[13]
Citation Linkwww.ebi.ac.ukPDBsum
Sep 29, 2019, 1:58 PM
[14]
Citation Linkwww.ncbi.nlm.nih.govarticles
Sep 29, 2019, 1:58 PM
[15]
Citation Linkwww.ncbi.nlm.nih.govarticles
Sep 29, 2019, 1:58 PM
[16]
Citation Linkwww.ncbi.nlm.nih.govproteins
Sep 29, 2019, 1:58 PM
[17]
Citation Linkenzyme.expasy.org4.2.1.135
Sep 29, 2019, 1:58 PM
[18]
Citation Linkdoi.org10.1074/jbc.m511021200
Sep 29, 2019, 1:58 PM
[19]
Citation Linkwww.ncbi.nlm.nih.gov16286454
Sep 29, 2019, 1:58 PM
[20]
Citation Linkwww.ncbi.nlm.nih.gov"In vitro biosynthesis of UDP-N,N'-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system"
Sep 29, 2019, 1:58 PM