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Information on EC 2.4.1.201 - alpha-1,6-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase and Organism(s) Homo sapiens

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IUBMB Comments
Requires a high concentration of Mn2+ for maximal activity. The enzyme, characterized from hen oviduct membranes, participates in the processing of N-glycans in the Golgi apparatus. It transfers GlcNAc in beta1-4 linkage to a D-mannose residue that already has GlcNAc residues attached at positions 2 and 6 by beta linkages. No homologous enzyme appears to exist in mammals.
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Homo sapiens
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
gnt vi, mgat6, n-acetylglucosaminyltransferase vi, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-glycopeptide beta-1,4-, VI
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acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-glycopeptide beta-1-4-, VI
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GCNT6
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GnT VI
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GnT-VI
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mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase
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Mgat6
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N-acetylglucosaminyltransferase VI
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase VI
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UDP-GlcNAc: GlcNAcbeta1-6(GlcNAcbeta1-2)Manalpha1-R [GlcNAc to Man] beta1-4N-acetylglucosaminyltransferase VI
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uridine diphosphoacetylglucosamine-glycopeptide beta-1-4-acetylglucosaminyltransferase VI
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-glucosamine:N-acetyl-beta-D-glucosaminyl-(1->6)-[N-acetyl-beta-D-glucosaminyl-(1->2)]-alpha-D-mannosyl-glycoprotein 4-beta-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Requires a high concentration of Mn2+ for maximal activity. The enzyme, characterized from hen oviduct membranes, participates in the processing of N-glycans in the Golgi apparatus. It transfers GlcNAc in beta1-4 linkage to a D-mannose residue that already has GlcNAc residues attached at positions 2 and 6 by beta linkages. No homologous enzyme appears to exist in mammals.
CAS REGISTRY NUMBER
COMMENTARY hide
119699-68-2
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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 + 2,6-bis(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl-R
UDP + 2,4,6-tris(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl-R
show the reaction diagram
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additional information
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evaluation of a highly sensitive method for determination of the activity of GnT VI using a fl uorescently labeled tetraantennary oligosaccharide as an acceptor substrate. GnT VI stringently requires beta1,6-N-acetylglucosaminylation on the Manalpha1-6 arm (GnT V product, EC 2.4.1.155) as an acceptor substrate. Agalacto-triantennary oligosaccharide (GnT V product) can also be used as an alternate substrate
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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
UDP-N-acetyl-D-glucosamine + 2,6-bis(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl-R
UDP + 2,4,6-tris(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl-R
show the reaction diagram
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
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activates
Mg2+
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activates
Mn2+
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required, best divalent cation
additional information
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divalent cation-dependent enzyme activity, maximal activity with Mn2+. Co2+ and Mg 2+ can partially substitute for Mn2+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
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the enzyme contributes to the surface expression of CD133 through the processing of multiantennary N -linked glycans on CD133
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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GlcNAc and tet-induced Mgat6 increases the levels of many metabolites in HeLa cells, and HEK293 cells, and tet-induced Mgat5 changes in the N-glycan distributions, N-glycans profiles of transgenic HeLa cells, overview. Tet-inducible Mgat5 enhances amino acid uptake and growth in nutrient-poor conditions. The Mgat5, EC 2.4.1.155, product is the preferred acceptor for Mgat6, which adds a GlcNAcbeta1,4 branch that is not present in mammals, Mgat6 enhances functionality of N-glycan branching in mammalian cells
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene MGAT6, recombinant tet-inducible expression of Flag-tagged GlcNAcT-V in HeLa and HEK293 cells. Tet-induced Mgat6 HEK293 cells produce increased oligosaccharide levels also observed in HeLa cells, predicted to be the 2,2,4,6 tetra-, 4,2,2,4 tetra- and 4,2,2,4,6 penta-N-glycans, while native 4,2,2,6 tetra are reduced, N-glycans profiles of transgenic HeLa and HEK-293 cells, overview
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Abdel Rahman, A.; Ryczko, M.; Nakano, M.; Pawling, J.; Rodrigues, T.; Johswich, A.; Taniguchi, N.; Dennis, J.
Golgi N-glycan branching N-acetylglucosaminyltransferases I, V and VI promote nutrient uptake and metabolism
Glycobiology
25
225-240
2015
Homo sapiens
Manually annotated by BRENDA team
Taguchi, T.; Taniguchi, N.
A method for determination of UDP-GlcNAc: GlcNAcbeta1-6(GlcNAcbeta1-2)Manalpha1-R [GlcNAc to Man] beta1-4N-acetylglucosaminyltransferase VI activity
Methods Mol. Biol.
1022
299-305
2013
Homo sapiens
Manually annotated by BRENDA team