Literature summary for 2.7.1.60 extracted from

Yardeni, T.; Choekyi, T.; Jacobs, K.; Ciccone, C.; Patzel, K.; Anikster, Y.; Gahl, W.A.; Kurochkina, N.; Huizing, M.
Identification, tissue distribution, and molecular modeling of novel human isoforms of the key enzyme in sialic acid synthesis, UDP-GlcNAc 2-epimerase/ManNAc kinase (2011), Biochemistry, 50, 8914-8925.

Search for more literature for 2.7.1.60

Cloned(Commentary)

Cloned (Comment)	Organism
cloning of isozymes hGNE1-hGNE8, DNA and amino acid sequence determination and analysis, quantitative real-time PCR expression analysis and sequence comparisons	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cytosol	-	Homo sapiens	5829	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + N-acyl-D-mannosamine	Homo sapiens	-	ADP + N-acyl-D-mannosamine 6-phosphate	-	?
additional information	Homo sapiens	the enzyme is a bifunctional enzyme uridine diphosphate 1-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, i.e. UDP-GlcNAc 2-epimerase/ManNAc kinase or GNE. The N-terminal domain carries out UDP-GlcNAc epimerase function, whereas the C-terminal domain is responsible for ManNAc kinase activity	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9Y223	eight isozymes hGNE1-hGNE8 from differential splicing	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + N-acyl-D-mannosamine	-	Homo sapiens	ADP + N-acyl-D-mannosamine 6-phosphate	-	?
additional information	the enzyme is a bifunctional enzyme uridine diphosphate 1-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, i.e. UDP-GlcNAc 2-epimerase/ManNAc kinase or GNE. The N-terminal domain carries out UDP-GlcNAc epimerase function, whereas the C-terminal domain is responsible for ManNAc kinase activity	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
More	the GNE enzyme consists of two enzymatic domains, sequence comparisons, secondary structures, and modeling of isozymes hGNE1-hGNE8, hGNE2 and hGNE7 display a 31-residue N-terminal extension compared to hGNE1. hGNE3 and hGNE8 contain a 55 residue N-terminal deletion, and a 50-residue N-terminal extension compared to hGNE1	Homo sapiens

Synonyms

Synonyms	Comment	Organism
GNE	-	Homo sapiens
UDP-GlcNAc 2-epimerase/ManNAc kinase	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Homo sapiens

General Information

General Information	Comment	Organism
malfunction	enzyme mutations can cause sialuria and hereditary inclusion body myopathy. Sialuria patients have a heterozygous missense mutation affecting the allosteric site of GNE, leading to loss of feedback inhibition of GNE-epimerase activity by CMP-Neu5Ac, resulting in excessive sialic acid production. HIBM and its allelic Japanese disorder, distal myopathy with rimmed vacuoles, or DMRV, is an autosomal recessive neuromuscular disorder of adult onset, characterized byslowly progressive muscle weakness and atrophy	Homo sapiens
metabolism	UDP-GlcNAc 2-epimerase/ManNAc kinase (GNE) catalyzes the first two committed steps in sialic acid synthesis	Homo sapiens
additional information	epimerase enzymatic activity of isozymes GNE3 and GNE8 is likely absent, since the deleted fragment contains important substrate binding residues in homologous bacterial epimerases. Isozymes hGNE5-hGNE8 have a 53-residue deletion, which is assigned a role in substrate(UDP-GlcNAc) binding	Homo sapiens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)