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Information on EC 5.1.3.14 - UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing) and Organism(s) Methanococcus maripaludis and UniProt Accession Q6LZC4

for references in articles please use BRENDA:EC5.1.3.14
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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:
Methanococcus maripaludis
UNIPROT: Q6LZC4
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Word Map
The taxonomic range for the selected organisms is: Methanococcus maripaludis
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
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-D-glucosamine
UDP-N-acetyl-D-mannosamine
show the reaction diagram
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r
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KCl
200 mM, twofold stimualtion
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.36
UDP-N-acetyl-D-glucosamine
pH 8.5, 37°C
additional information
additional information
Hill coefficient of 2.7, positive cooperativity
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.4
UDP-N-acetyl-D-glucosamine
pH 8.5, 37°C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
101000
gel filtration
40000
2 * 40000, SDS-PAGE, 2 * 42400, calculated, recombinant enzyme
42400
2 * 40000, SDS-PAGE, 2 * 42400, calculated, recombinant enzyme
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 40000, SDS-PAGE, 2 * 42400, calculated, recombinant enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli, C-terminal His-tag
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Namboori, S.C.; Graham, D.E.
Acetamido sugar biosynthesis in the Euryarchaea
J. Bacteriol.
190
2987-2996
2008
Methanococcus maripaludis (Q6LZC4)
Manually annotated by BRENDA team