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Information on EC 5.1.3.14 - UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing) and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q58899

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IUBMB Comments
This bacterial enzyme catalyses the reversible interconversion of UDP-GlcNAc and UDP-ManNAc. The latter is used in a variety of bacterial polysaccharide biosyntheses. cf. EC 3.2.1.183, UDP-N-acetylglucosamine 2-epimerase (hydrolysing).
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This record set is specific for:
Methanocaldococcus jannaschii
UNIPROT: Q58899
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Word Map
The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
udp-n-acetylglucosamine 2-epimerase/n-acetylmannosamine kinase, udp-glcnac 2-epimerase, udp-n-acetylglucosamine 2-epimerase, udp-n-acetylglucosamine-2-epimerase/n-acetylmannosamine kinase, udp-glcnac 2-epimerase/mannac kinase, gne/mnk, cap5p, nmsaca, udp-glcnac-2-epimerase, udp-n-acetylglucosamine-2-epimerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
uridine diphosphate N-acetylglucosamine 2-epimerase
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Epimerase, uridine diphosphoacetylglucosamine 2-
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UDP-GlcNAc 2'-epimerase
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UDP-GlcNAc-2-epimerase
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UDP-N-acetylglucosamine 2'-epimerase
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Uridine diphosphate-N-acetylglucosamine-2'-epimerase
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Uridine diphospho-N-acetylglucosamine 2'-epimerase
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Uridine diphosphoacetylglucosamine 2'-epimerase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
epimerization
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-glucosamine 2-epimerase
This bacterial enzyme catalyses the reversible interconversion of UDP-GlcNAc and UDP-ManNAc. The latter is used in a variety of bacterial polysaccharide biosyntheses. cf. EC 3.2.1.183, UDP-N-acetylglucosamine 2-epimerase (hydrolysing).
CAS REGISTRY NUMBER
COMMENTARY hide
9037-71-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
show the reaction diagram
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r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
UDP
binding structure, overview
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
mutation of this enzyme causes changes in cell morphology and the thermoresistance of the cell wall
metabolism
the enzyme catalyzes the interconversion of UDP-N-acetyl-alpha-D-glucosamine to UDP-N-acetyl-alpha-D-mannosamine, which is used in the biosynthesis of cell surface polysaccharides in bacteria
physiological function
UDP-GlcNAc 2-epimerase catalyzes the interconversion of UDP-GlcNAc to UDP-ManNAc, which is used in the biosynthesis of cell surface polysaccharides in bacteria
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapor-diffusion method, crystal structures in open and closed conformations. A comparison of these crystal structures shows that upon UDP and UDPGlcNAc binding, the enzyme undergoes conformational changes involving a rigid-body movement of the C-terminal domain
UDP-GlcNAc 2-epimerase in open and closed conformations, and UDP-GlcNAc 2-epimerase in complex with UDPGlcNAc and UDP, sitting drop vapor diffusion method, mixing of 0.001 ml of 5 mg/ml protein in 50 mM Tris-HCl, pH 8.0, 100 mM NaCl, 5% glycerol, and 2 mM tris(2-carboxyethyl)phosphine, with 0.001 ml of reservoir solution containing 40 mM Tris-propane, 60 mM citrate, pH 4.1, and 16% PEG3350, and equilibration against 0.3 ml of reservoir solution at 20°C for 1 week, X-ray diffraction structure determination and analysis at 1.42-2.85 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography, gel filtration, and ultrafiltration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene wecB, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chen, S.C.; Huang, C.H.; Shin Yang, C.; Liu, J.S.; Kuan, S.M.; Chen, Y.
Crystal structures of the archaeal UDP-GlcNAc 2-epimerase from Methanocaldococcus jannaschii reveal a conformational change induced by UDP-GlcNAc
Proteins
82
1519-1526
2014
Methanocaldococcus jannaschii (Q58899), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58899)
Manually annotated by BRENDA team
Chen, S.; Huang, C.; Shin Yang, C.; Liu, J.; Kuan, S.; Chen, Y.
Crystal structures of the archaeal UDP-GlcNAc 2-epimerase from Methanocaldococcus jannaschii reveal a conformational change induced by UDP-GlcNAc
Proteins
82
1519-1526
2014
Bacillus subtilis (P39131), Bacillus subtilis, Bacillus subtilis 168 (P39131), Methanocaldococcus jannaschii (Q58899), Methanocaldococcus jannaschii
Manually annotated by BRENDA team