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Information on EC 2.7.1.60 - N-acylmannosamine kinase and Organism(s) Mus musculus and UniProt Accession Q91WG8

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IUBMB Comments
Acts on the acetyl and glycolyl derivatives.
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This record set is specific for:
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
n-acetylmannosamine kinase, udp-glcnac 2-epimerase/mannac 6-kinase, udp-n-acetylglucosamine-2-epimerase/n-acetylmannosamine-kinase, n-acyl-d-mannosamine kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
UDP-GlcNAc 2-epimerase/ManNAc kinase
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UDP-GlcNAc-epimerase/ManNAc kinase
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acetylamidodeoxymannokinase
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acetylmannosamine kinase
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acylaminodeoxymannokinase
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acylmannosamine kinase
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acylmannosamine kinase (phosphorylating)
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ATP:N-acetylmannosamine 6-phosphotransferase
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EC 2.7.1.59/EC 2.7.1.60
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bifunctional, N-acetylglucosamine kinase and N-acetylmannosamine kinase activity
N-acetylmannosamine kinase
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N-acyl-D-mannosamine kinase
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UDP-GlcNAc 2-epimerase/ManNAc kinase
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UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
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two different enzyme activities combined in a single bifunctional enzyme
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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SYSTEMATIC NAME
IUBMB Comments
ATP:N-acyl-D-mannosamine 6-phosphotransferase
Acts on the acetyl and glycolyl derivatives.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-53-6
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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
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
show the reaction diagram
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-
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine-6-phosphate
show the reaction diagram
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-
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
show the reaction diagram
additional information
?
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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
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
show the reaction diagram
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-
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
show the reaction diagram
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key enzyme in the synthesis of N-acetylneuraminic acid and therefore of nearly all other sialic acids, essential for early embryonic development
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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homozygous or heterozygous gene knock-out cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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associated
Manually annotated by BRENDA team
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associated
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
sequence comparion and modeling of human hGNE1 and mouse mGne1 isozymmess, overview
malfunction
non-allosteric GNE gene mutations cause the muscular disorder GNE myopathy, i.e. hereditary inclusion body myopathy. Complete Gne knockout is embryonically lethal. Transgenic mice expressing the human GNE cDNA with the D176V mutation, common among Japanese patients, in a mouse background with a disrupted mouse Gne gene recapitulates the adult onset features of human GNE myopathy with hyposialylation in serum and different organs. M712T mouse mutants die within 72 h of birth from severe glomerular disease. Mouse isozyme mutant phenotypes, overview
metabolism
the bifunctional enzyme UDP-GlcNAc 2-epimerase/ManNAc kinase, GNE, catalyzes the first two committed steps in sialic acid synthesis
physiological function
the mGne2 encoding transcript is differentially expressed and may act as a tissue-specific regulator of sialylation. mGne2 expression appears significantly increased the first 2 days of life, possibly reflecting the high sialic acid demand during this period
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)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000
Western blot analysis
37300
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amino acid sequence, predicted from an open reading frame
79000
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x * 79000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 79000, SDS-PAGE
additional information
the GNE enzyme consists of two enzymatic domains, sequence comparisons, secondary structures, and modeling of isozymes mGNE1 and mGNE2
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D176V
oral administration of the sialic acid precursor N-acetylmannosamine rescues the muscle phenotype in the transgenic Gne p.D176V mouse and partially rescues the glomerular disease and early lethality in the knockin Gne mutant M712T mouse model
M712T
naturally occuring mutation of isozyme mGne2. Tissues of the knock-in Gne p.M712T mouse model has similar mGne transcript expression levels among genotypes, indicating no effect of the mutation on mRNA expression, but the mutant shows increased activity in presence of N-acetylmannosamine compared to the wild-type enzyme. M712T mouse mutants die within 72 h of birth from severe glomerular disease
additional information
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heterozygous mice deficient for bifunctional UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase display a organ-specific reduction of membrane-bound sialic acids of about 25%. Transferrin expression is unchanged in heterozygous mice, but the isoelectric point of transferrin is shifted towards basic pH value. The expression of polysialic acids on polysialylated neural cell adhesion molecule is reduced
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA cloned and sequenced, expressed in Escherichia coli HB101 or INValphaF'
cloning of isozymes mGNE1 and mGNE2, DNA and amino acid sequence determination and analysis, quantitative real-time PCR expression analysis and sequence comparison
cloned and functionally expressed in Escherichia coli BL21
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hinderlich, S.; Berger, M.; Schwarzkopf, M.; Effertz, K.; Reutter, W.
Molecular cloning and characterization of murine and human N-acetylglucosamine kinase
Eur. J. Biochem.
267
3301-3308
2000
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Horstkorte, R.; Noehring, S.; Wiechens, N.; Schwarzkopf, M.; Danker, K.; Reutter, W.; Lucka, L.
Tissue expression and amino acid sequence of murine UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase
Eur. J. Biochem.
260
923-927
1999
Mus musculus (Q91WG8), Mus musculus NMRI (Q91WG8), Rattus norvegicus, Rattus norvegicus Wistar
Manually annotated by BRENDA team
Krause, S.; Hinderlich, S.; Amsili, S.; Horstkorte, R.; Wiendl, H.; Argov, Z.; Mitrani-Rosenbaum, S.; Lochmueller, H.
Localization of UDP-GlcNAc 2-epimerase/ManAc kinase (GNE) in the Golgi complex and the nucleus of mammalian cells
Exp. Cell Res.
304
365-379
2005
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Gagiannis, D.; Orthmann, A.; Danssmann, I.; Schwarzkopf, M.; Weidemann, W.; Horstkorte, R.
Reduced sialylation status in UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase (GNE)-deficient mice
Glycoconj. J.
24
125-130
2007
Mus musculus
Manually annotated by BRENDA team
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 (Q91WG8)
Manually annotated by BRENDA team