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Information on EC 3.2.1.183 - UDP-N-acetylglucosamine 2-epimerase (hydrolysing) and Organism(s) Mus musculus and UniProt Accession Q91WG8

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IUBMB Comments
The enzyme is found in mammalian liver, as well as in some pathogenic bacteria including Neisseria meningitidis and Staphylococcus aureus. It catalyses the first step of sialic acid (N-acetylneuraminic acid) biosynthesis. The initial product formed is the alpha anomer, which rapidly mutarotates to a mixture of anomers . The mammalian enzyme is bifunctional and also catalyses EC 2.7.1.60, N-acetylmannosamine kinase. cf. EC 5.1.3.14, UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing).
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Mus musculus
UNIPROT: Q91WG8
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The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
bifunctional udp-n-acetylglucosamine 2-epimerase/n-acetylmannosamine kinase, bifunctional udp-glcnac 2-epimerase/mannac kinase, uridine diphosphate-n-acetylglucosamine-2-epimerase, uridine diphosphate-n-acetylglucosamine 2-epimerase/n-acetylmannosamine kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
UDP-GlcNAc 2-epimerase/ManNAc kinase
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neuC
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-
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siaA
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-
-
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UDP-GlcNAc 2-epimerase/ManNAc kinase
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-glucosamine hydrolase (2-epimerising)
The enzyme is found in mammalian liver, as well as in some pathogenic bacteria including Neisseria meningitidis and Staphylococcus aureus. It catalyses the first step of sialic acid (N-acetylneuraminic acid) biosynthesis. The initial product formed is the alpha anomer, which rapidly mutarotates to a mixture of anomers [2]. The mammalian enzyme is bifunctional and also catalyses EC 2.7.1.60, N-acetylmannosamine kinase. cf. EC 5.1.3.14, UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isozyme mGne1
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
GNE myopathy is autosomal recessive inherited and characterized by adult onset, slowly progressive muscle weakness and atrophy
physiological function
mGne2 encoding transcript may act as a tissue-specific regulator of sialylation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GLCNE_MOUSE
722
0
79199
Swiss-Prot
other Location (Reliability: 5)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Gne1, sequence comparison with the human isozyme Gne1
gene Gne2, sequence comparison with the human isozyme Gne2
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
treatment of knock-in Gne p.M712T mouse model with N-acetylmannosamine, the Gne transcript expression, in particular mGne2, increases significantly, likely resulting in increased Gne enzymatic activities, especially in kidney and skeletal muscle
treatment of knock-in Gne p.M712T mouse model with N-acetylmannosamine, the Gne transcript expression, in particular mGne2, increases significantly, likely resulting in increased Gne enzymatic activities, especiallyin kidney and skeletal muscle
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yardeni, T.; Jacobs, K.; Niethamer, T.K.; Ciccone, C.; Anikster, Y.; Kurochkina, N.; Gahl, W.A.; Huizing, M.
Murine isoforms of UDP-GlcNAc 2-epimerase/ManNAc kinase: secondary structures, expression profiles, and response to ManNAc therapy
Glycoconj. J.
30
609-618
2013
Mus musculus (Q3UW64), Mus musculus (Q91WG8), Mus musculus C57/BL6J (Q3UW64), Mus musculus C57/BL6J (Q91WG8)
Manually annotated by BRENDA team