UDP-N-acetylglucosamine 4,6-dehydratase (configuration-retaining)
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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) | |||||||||
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Identifiers | |||||||||
EC number | 4.2.1.135 [4] | ||||||||
Databases | |||||||||
IntEnz | IntEnz view [5] | ||||||||
BRENDA | BRENDA entry [6] | ||||||||
ExPASy | NiceZyme view [7] | ||||||||
KEGG | KEGG entry [8] | ||||||||
MetaCyc | metabolic pathway [9] | ||||||||
PRIAM | profile [10] | ||||||||
PDB structures | RCSB PDB [11] PDBe [12] PDBsum [13] | ||||||||
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Search | |||||||||
PMC | articles [14] | ||||||||
PubMed | articles [15] | ||||||||
NCBI | proteins [16] |
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-glucosamine
This enzyme contains NAD+ as a cofactor.
UDP-N-acetylglucosamine 4,6-dehydratase (configuration-retaining) | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC number | 4.2.1.135 [4] | ||||||||
Databases | |||||||||
IntEnz | IntEnz view [5] | ||||||||
BRENDA | BRENDA entry [6] | ||||||||
ExPASy | NiceZyme view [7] | ||||||||
KEGG | KEGG entry [8] | ||||||||
MetaCyc | metabolic pathway [9] | ||||||||
PRIAM | profile [10] | ||||||||
PDB structures | RCSB PDB [11] PDBe [12] PDBsum [13] | ||||||||
| |||||||||
Search | |||||||||
PMC | articles [14] | ||||||||
PubMed | articles [15] | ||||||||
NCBI | proteins [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
[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