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Information on EC 2.4.1.145 - alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase
for references in articles please use BRENDA:EC2.4.1.145
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.145 alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase
IUBMB Comments
Requires Mn2+. The enzyme, found in vertebrates, participates in the processing of N-glycans in the Golgi apparatus. By adding a glucosaminyl residue to biantennary N-linked glycans, it enables the synthesis of tri- and tetra-antennary complexes.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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Synonyms
gnt-iv, gnt-iva, mgat4a, gnt-ivb, n-acetylglucosaminyltransferase iv, mgat4b, gnt iv, n-acetylglucosaminyltransferase-iv, glcnactase-iv, n-acetylglucosaminyltransferase-iva, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-1,3-mannosylglycoprotein beta-1,4-N-acetylglucosaminyltransferase
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beta-acetylglucosaminyltransferase IV
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EC 2.4.1.51
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formerly, part transferred
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GnT-IV
GnT-IVa
GnT-IVb
GnTIVa
Mgat4a
Mgat4b
N-acetylglucosaminyltransferase IV
N-acetylglucosaminyltransferase IVa
N-acetylglucosaminyltransferase-IV
N-acetylglucosaminyltransferase-IVa
N-acetylglucosaminyltransferase-IVb
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IV
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uridine diphosphoacetylglucosamine-glycopeptide beta4-acetylglucosaminyltransferase IV
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N-acetylglucosaminyltransferase IV
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein] = UDP + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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PATHWAY SOURCE
PATHWAYS
MetaCyc
complex N-linked glycan biosynthesis (vertebrates)
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-glucosamine:N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-beta-D-mannosyl-glycoprotein 4-beta-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Requires Mn2+. The enzyme, found in vertebrates, participates in the processing of N-glycans in the Golgi apparatus. By adding a glucosaminyl residue to biantennary N-linked glycans, it enables the synthesis of tri- and tetra-antennary complexes.
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CAS REGISTRY NUMBER
COMMENTARY
86498-16-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-Fmoc
UDP + ?
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-Fmoc
UDP + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-Fmoc
Substrates: optimal substrate
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[integrin beta1]
UDP + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[integrin beta1]
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[lysosome-associated membrane glycoprotein 2]
UDP + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[lysosome-associated membrane glycoprotein 2]
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
UDP + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-L-Fuc-(1->6)]-beta-D-GlcNAc-N-Asn-Fmoc
UDP + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-L-Fuc-(1->6)]-beta-D-GlcNAc-N-Asn-Fmoc
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-glucosamine + pyridylaminated acceptor substrate
?
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Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP-N-acetyl-D-glucosamine + biantennary N-glycan
?
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Substrates: the enzyme transfers a N-acetyl-D-glucosamine from UDP-N-acetyl-D-glucosamine to the biantennary oligosaccharide and produces triantennary N-glycans with a beta1,4-N-acetyl-D-glucosamine on the alpha1,3-Man arm
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta1-2(GlcNAcbeta1-6)Manalpha1-6(GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta1-2Manalpha1-3(GlcNAcbeta1-2Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta1-2Manalpha1-3(GlcNAcbeta1-2Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
UDP + ?
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Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta1-2Manalpha1-3(Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta1-2Manalpha1-6(GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
?
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Substrates: isozyme GnT-IVb has about 30% activity of isozyme GnT-IVa
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[lysosome-associated membrane glycoprotein 2]
UDP + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[lysosome-associated membrane glycoprotein 2]
Substrates: i.e. LAMP-2, LAMP-2 has 16 N-glycans which play crucial roles in cell adhesion to ECM and metastasis of cancer cells because N-glycans configure cell surface ligands of cancer cells for galectin-1, galectin-3, and selectins on extracellular matrix or the membranes of the counter cell
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[lysosome-associated membrane glycoprotein 2]
UDP + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[lysosome-associated membrane glycoprotein 2]
Substrates: i.e. LAMP-2
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
Substrates: maximal activity requires the presence of both terminal beta-1,2-linked N-acetylglucosamine residues in the substrate
Products: -
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?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
-
Substrates: -
Products: -
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?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
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Substrates: maximal activity requires the presence of both terminal beta-1,2-linked N-acetylglucosamine residues in the substrate
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
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Substrates: R represents the remainder of the N-oligosaccharide in the glycoprotein acceptor, the enzyme adds N-cetylglucosamine in beta-1,4-linkage to the alpha-1,3-linked mannosyl residues of the trimannosyl core of N-glycosyloligosaccharides
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?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
-
Substrates: -
Products: -
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?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
Substrates: -
Products: -
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?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
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Substrates: the enzyme is involved in the branch formation of Asn-linked sugar chains
Products: -
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?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
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Substrates: GnT-IVa is primarily responsible for the biosynthesis of complex-type N-glycans
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?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
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Substrates: GnT-IVb might contribute to the basal GnT-IV activity in cells
Products: -
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?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
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Substrates: pyridylaminated sugar chain
Products: -
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?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta1-2(GlcNAcbeta1-6)Manalpha1-6(GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
?
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Substrates: N-acetylglucosaminyltransferase-IVa
Products: -
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?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta1-2(GlcNAcbeta1-6)Manalpha1-6(GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
?
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Substrates: N-acetylglucosaminyltransferase-IVb
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta1-2Manalpha1-3(GlcNAcbeta1-2Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
?
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Substrates: N-acetylglucosaminyltransferase-IVa
Products: -
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?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta1-2Manalpha1-3(GlcNAcbeta1-2Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
?
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Substrates: N-acetylglucosaminyltransferase-IVb
Products: -
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?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta1-2Manalpha1-3(Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
?
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Substrates: N-acetylglucosaminyltransferase-IVa
Products: -
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UDP-N-acetyl-D-glucosamine + GlcNAcbeta1-2Manalpha1-3(Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
?
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Substrates: N-acetylglucosaminyltransferase-IVb
Products: -
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?
additional information
?
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Substrates: the enzyme transfers a GlcNAc to the alpha-1,3 mannose arm of the biantennary N-glycan GlcNAc2Man3GlcNAc2 to form a beta-1,4 GlcNAc branched structure
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additional information
?
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Substrates: the enzyme can transfer GlcNAc from UDP-GlcNAc to the alpha1,3-Man arm of an N-glycan via a beta1,4-linkage
Products: -
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additional information
?
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Substrates: the enzyme can transfer GlcNAc from UDP-GlcNAc to the alpha1,3-Man arm of an N-glycan via a beta1,4-linkage
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additional information
?
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Substrates: GnT-IVa and GnT-IVb have distinct glycoprotein preferences. GnT-IVb acts efficiently on glycoproteins bearing an N-glycan premodified by GnT-IV. Haptoglobin, alpha1 antitrypsin, and transferrin are the best three substrates for GnT-IVa. The C-terminal lectin domain regulates differential substrate selectivity of GnT-IVa and GnT-IVb. The larger glycoproteins (over 150 kDa) are efficiently modified by GnT-IVa, whereas proteins at 75 kDa are modified by GnT-IVb. GnT-IVa exhibits high activity toward asialoagalacto forms of transferrin, haptoglobin, and alpha1 antitrypsin and shows signals comparable to or less than that of the oligosaccharide substrate GnGnbi-PA for the poor glycoprotein substrates (alpha1-acid glycoprotein, fibrinogen, and IgG). GnT-IVb displays higher activity toward all the glycoproteins than towards the oligosaccharide substrate GnGnbi-PA, with a markedly higher preference for haptoglobin and alpha1-acid glycoprotein
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additional information
?
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Substrates: GnT-IVa and GnT-IVb have distinct glycoprotein preferences. GnT-IVb acts efficiently on glycoproteins bearing an N-glycan premodified by GnT-IV. Haptoglobin, alpha1 antitrypsin, and transferrin are the best three substrates for GnT-IVa. The C-terminal lectin domain regulates differential substrate selectivity of GnT-IVa and GnT-IVb. The larger glycoproteins (over 150 kDa) are efficiently modified by GnT-IVa, whereas proteins at 75 kDa are modified by GnT-IVb. GnT-IVa exhibits high activity toward asialoagalacto forms of transferrin, haptoglobin, and alpha1 antitrypsin and shows signals comparable to or less than that of the oligosaccharide substrate GnGnbi-PA for the poor glycoprotein substrates (alpha1-acid glycoprotein, fibrinogen, and IgG). GnT-IVb displays higher activity toward all the glycoproteins than towards the oligosaccharide substrate GnGnbi-PA, with a markedly higher preference for haptoglobin and alpha1-acid glycoprotein
Products: -
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additional information
?
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Substrates: the enzyme can transfer GlcNAc from UDP-GlcNAc to the alpha1,3-Man arm of an N-glycan via a beta1,4-linkage
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additional information
?
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Substrates: the enzyme can transfer GlcNAc from UDP-GlcNAc to the alpha1,3-Man arm of an N-glycan via a beta1,4-linkage
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[lysosome-associated membrane glycoprotein 2]
UDP + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[lysosome-associated membrane glycoprotein 2]
Substrates: i.e. LAMP-2, LAMP-2 has 16 N-glycans which play crucial roles in cell adhesion to ECM and metastasis of cancer cells because N-glycans configure cell surface ligands of cancer cells for galectin-1, galectin-3, and selectins on extracellular matrix or the membranes of the counter cell
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
UDP + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
Substrates: -
Products: -
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UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
additional information
?
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Substrates: the enzyme transfers a GlcNAc to the alpha-1,3 mannose arm of the biantennary N-glycan GlcNAc2Man3GlcNAc2 to form a beta-1,4 GlcNAc branched structure
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UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
-
Substrates: -
Products: -
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?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
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Substrates: the enzyme is involved in the branch formation of Asn-linked sugar chains
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
-
Substrates: GnT-IVa is primarily responsible for the biosynthesis of complex-type N-glycans
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
-
Substrates: GnT-IVb might contribute to the basal GnT-IV activity in cells
Products: -
Products: -
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
10 mM, about 10% of the activity compared to activity in presence of 10 mM Mn2+
Co2+
Mg2+
Mn2+
Co2+
10 mM, about 50% of the activity compared to activity in presence of 10 mM Mn2+
Mg2+
10 mM, about 40% of the activity compared to activity in presence of 10 mM Mn2+
Mn2+
maximum activity with 5 mM Mn2+ at 37°C in MES/NaOH (pH 7.0). The recombinant protein has the highest catalytic activity in the presence of Mn2+ and that the activity gradually decreased when Co2+, Mg2+, and Ca2+ are present
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
sugar nucleotides having the UDP moiety inhibit activity to different extent
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
alpha-1,3-mannosyl-glycoprotein 4-beta-n-acetylglucosaminyltransferase deficiency
Physiological and glycomic characterization of N-acetylglucosaminyltransferase-IVa and -IVb double deficient mice.
Carcinoma, Hepatocellular
Determination of N-acetylglucosaminyltransferases III, IV and V in normal and hepatoma tissues of rats.
Choriocarcinoma
High expression of N-acetylglucosaminyltransferase IVa promotes invasion of choriocarcinoma.
Choriocarcinoma
Structural differences found in the asparagine-linked sugar chains of human chorionic gonadotropins purified from the urine of patients with invasive mole and with choriocarcinoma.
Choriocarcinoma
Structure, pathology and function of the N-linked sugar chains of human chorionic gonadotropin.
Choriocarcinoma
Unusually high expression of N-acetylglucosaminyltransferase-IVa in human choriocarcinoma cell lines: a possible enzymatic basis of the formation of abnormal biantennary sugar chain.
Diabetes Mellitus, Type 2
Targeted genetic inactivation of N-acetylglucosaminyltransferase-IVa impairs insulin secretion from pancreatic beta cells and evokes type 2 diabetes.
Diabetes Mellitus, Type 2
The transcription of MGAT4A glycosyl transferase is increased in white cells of peripheral blood of Type 2 Diabetes patients.
Hydatidiform Mole, Invasive
N-acetylglucosaminyltransferase IVa promotes invasion of choriocarcinoma.
Lung Neoplasms
Multiplexed surrogate analysis of glycotransferase activity in whole biospecimens.
Neoplasm Metastasis
N-acetylglucosaminyltransferase IVa regulates metastatic potential of mouse hepatocarcinoma cells through glycosylation of CD147.
Neoplasms
Aberrant expression of N-acetylglucosaminyltransferase-IVa and IVb (GnT-IVa and b) in pancreatic cancer.
Neoplasms
Glycans and cancer: role of N-glycans in cancer biomarker, progression and metastasis, and therapeutics.
Neoplasms
Identification of hub genes and key pathways associated with the progression of gynecological cancer.
Neoplasms
Kinetic properties and substrate specificities of two recombinant human N-acetylglucosaminyltransferase-IV isozymes.
Neoplasms
Unusually high expression of N-acetylglucosaminyltransferase-IVa in human choriocarcinoma cell lines: a possible enzymatic basis of the formation of abnormal biantennary sugar chain.
Pancreatic Neoplasms
Aberrant expression of N-acetylglucosaminyltransferase-IVa and IVb (GnT-IVa and b) in pancreatic cancer.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.532 - 3.35
GlcNAcbeta1-2(GlcNAcbeta1-6)Manalpha1-6(GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
1.04 - 6.94
GlcNAcbeta1-2Man1-3(GlcNAcbeta1-2Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
0.971 - 5.72
GlcNAcbeta1-2Manalpha1-3(GlcNAcbeta1-2Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
3.19 - 10.5
GlcNAcbeta1-2Manalpha1-3(Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
0.532
GlcNAcbeta1-2(GlcNAcbeta1-6)Manalpha1-6(GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
-
37°C, pH 7.5, recombinant full-length N-acetylglucosaminyltransferase-IVa
3.35
GlcNAcbeta1-2(GlcNAcbeta1-6)Manalpha1-6(GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
-
37°C, pH 7.5, recombinant full-length N-acetylglucosaminyltransferase-IVb
1.04
GlcNAcbeta1-2Man1-3(GlcNAcbeta1-2Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
-
37°C, pH 7.5, recombinant soluble human flag-GnTIVa
6.94
GlcNAcbeta1-2Man1-3(GlcNAcbeta1-2Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
-
37°C, pH 7.5, recombinant soluble human flag-GnTIVa
0.971
GlcNAcbeta1-2Manalpha1-3(GlcNAcbeta1-2Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
-
37°C, pH 7.5, recombinant full-length N-acetylglucosaminyltransferase-IVa
5.72
GlcNAcbeta1-2Manalpha1-3(GlcNAcbeta1-2Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
-
37°C, pH 7.5, recombinant full-length N-acetylglucosaminyltransferase-IVb
3.19
GlcNAcbeta1-2Manalpha1-3(Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
-
37°C, pH 7.5, recombinant full-length N-acetylglucosaminyltransferase-IVa
10.5
GlcNAcbeta1-2Manalpha1-3(Manalpha1-6)Manbeta1-4GlcNAcbeta1-4GlcNAc-2-aminopyridine
-
37°C, pH 7.5, recombinant full-length N-acetylglucosaminyltransferase-IVb
0.118
UDP-N-acetyl-D-glucosamine
-
37°C, pH 7.5, recombinant full-length N-acetylglucosaminyltransferase-IVa
0.242
UDP-N-acetyl-D-glucosamine
-
37°C, pH 7.5, recombinant full-length N-acetylglucosaminyltransferase-IVb
0.341
UDP-N-acetyl-D-glucosamine
-
37°C, pH 7.5, recombinant soluble human flag-GnTIVa
0.358
UDP-N-acetyl-D-glucosamine
-
37°C, pH 7.5, recombinant soluble human flag-GnTIVa
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
comparison between normal and malignant chorionic cells
additional information
-
comparison between normal and malignant pancreatic cells
additional information
differences between isozymes expressed in COS7 cells
additional information
-
comparison between normal and malignant kidney cortex cells
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.3
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
pH 6.0: about 50% of maximal activity, pH 8.0: about 35% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 45
15°C: about 50% of maximal activity, 45°C: about 45% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
isoform GnT-IVa is highly restricted in gastrointestinal organs and peripheral blood leukocytes
brenda
high expression of GnT-IVa, profiles and structures of the cell-surface N-glycan of hepatocellular carcinoma cells, high levels of NA3Fb, a core-alpha-1,6-fucosylated triantennary glycan, overview
brenda
-
isoform GnT-IVa is highly restricted in gastrointestinal organs and peripheral blood leukocytes
brenda
additional information
in epirubicin-resistant HLE cells, GnT-IVa expression is decreased
brenda
in epirubicin-resistant HLE cells, GnT-IVb expression is increased
brenda
Panc-1, PCI6, MIA PaCa-2, and BxPC3. Down-regulation of GnT-IVa in pancreatic cancer cells is due to an epigenetic abnormality in the gene. When pancreatic cancer cells are treated with 5-aza-C or butyrate, the expression of GnT-IVa is dramatically increased
brenda
Panc-1, PCI6, MIA PaCa-2, and BxPC3. Expression of GnT-IVb is increased in pancreatic cancer, compared to normal pancreatic tissues
brenda
additional information
-
isoform GnT-IVb is ubiquitously and constitutively expressed among tissues
brenda
additional information
-
in wild type mice, GnT-IVa expression is restricted to gastrointestinal tissues, whereas GnT-IVb is broadly expressed among organs
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
-
isozyme GnT-IVb deficiency shows mild phenotypic alterations in hematopoietic cell populations and hemostasis, GnT-IVa/-IVb double deficiency completely abolishes GnT-IV activity that results in the disappearance of the GlcNAcbeta1-4 branch on the Manalpha1-3 arm
malfunction
aberrant glycosylation of the cell surface is associated with the malignant transformation of normal cells. Tumor-cell-surface glycans are closely associated with tumor-cell migration, adhesion, and metastasis4, profiling of specific cell surface N-glycans in hepatocellular carcinoma with clinical tissues (88 tumor and adjacent normal tissues) and the corresponding serum samples of hepatocellular carcinoma patients, overview. The level of core-alpha-1,6-fucosylated triantennary glycan (NA3Fb) increases both on the cell surface and in the serum samples of hepatocellular carcinoma patients, and mRNA and protein expression of N-acetylglucosaminyltransferase IVa (GnT-IVa), which is related to the synthesis of the NA3Fb, is substantially increased in hepatocellular carcinoma tissues. Knockdown of GnT-IVa leads to a decreased level of NA3Fb and decreased ability of invasion and migration in HCC cells. The high expression of GnT-IVa is the cause of the abnormal increase of NA3Fb on the HCC cell surface, which regulates cell migration
malfunction
GnT-IVa overexpression increases cell adhesion, migration and invasion abilities of Jar cells. GnT-IVa overexpression increases cellular interaction with ECM as demonstrated by the relative adhesion rates of mock cells and Jar-GnT4a cells on fibronectin, collagen type I and collagen type IV. GnT-IVa knockdown in choriocarcinoma cells suppresses migration and invasion and decreases cellular adhesion to extracellular matrix
malfunction
GnT-IVb KO mice do not show any obvious physical or reproductive defects, but have slightly increased glucose and aspartate aminotransferase levels in the blood. GnT-IVa and GnT-IVb double KO mice completely lose GnT-IV activity in all tissues tested, and the phenotype of double KO mice is similar to that of GnT-IVa single KO mice
metabolism
-
N-acetylglucosaminyltransferase-IV synthesizes the GlcNAcbeta(1-4) branch structure on the Manalpha(1-3) arm of N-glycan core, and is essential for the production of multiantennary N-glycans cooperatively with N-acetylglucosaminyltransferase-V
metabolism
-
N-acetylglucosaminyltransferase-IV synthesizes the GlcNAcbeta(1-4) branch structure on the Manalpha(1-3) arm of N-glycan core, and is essential for the production of multiantennary N-glycans cooperatively with N-acetylglucosaminyltransferase-V
metabolism
hepatitis C virus infection inhibits GLUT2 N-glycosylation on the pancreatic beta cell surface by downregulating the expression of GnT-IVa and then activates the ATP-sensitive potassium channel pathway, which ultimately leads to disturbances in insulin secretion
physiological function
-
the enzyme acts in migration and metastasis of mouse hepatocarcinoma cells through altering the glycosylation of CD147
physiological function
the enzyme is involved in synthesis of tetra-antennary N-linked glycans. Cell surface glycans play an important role in intercellular and intracellular processes, including cell adhesion and development, cell recognition, and cancer development and metastasis. Changes in cell surface glycosylation modulate cellular activity
physiological function
N-acetylglucosaminyltransferase IV (GnT-IV) is a glycosyltransferase which catalyses the formation of beta1,4GlcNAc branches on the mannose core of N-glycans. beta1,4GlcNAc branches on human chorionic gonadotropin (hCG) are detected in GTN but not in normal pregnancy or hydatidiform mole. N-acetylglucosaminyltransferase IVa promotes invasion of choriocarcinoma. Identification of target proteins for GnT-IVa glycosylation which contribute to the malignancy of choriocarcinoma, overview. GnT-IVa overexpression increases highly branched N-glycans on integrin beta1. Highly branched N-glycans resulting from the action of GnT-IVa are strongly detected in invasive mole and choriocarcinoma, in proportion to the GnT-IVa protein expression. GnT-IVa may play an important role in accelerating the malignancy of choriocarcinoma through addition of beta1,4GlcNAc branches to the N-glycans on some proteins
physiological function
key transferase that catalyzes the formation of beta1,4 N-acetylglucosamine branches on the mannose core of N-glycans. N-Acetylglucosaminyltransferase IVa is involved in hepatocellular carcinoma metastasis by forming N-glycans. GnT-IVa can promote hepatocellular carcinoma cell motility by affecting the biological functions of ITGB1 through N-glycosylation
physiological function
GnT-IVa and GnT-IVb have glycosyltransferase activity that generates the type-2 diabetes-related beta1,4-GlcNAc branch on the alpha1,3-Man arm of N-glycans
physiological function
the enzyme promotes tumor growth in mice. This effect is attenuated after mutating the enzymatic site (D445A) of GnT-IVa, suggesting that GnT-IVa regulates hepatocellular carcinoma progression by forming beta1,4GlcNAc branches. GnT-IVa can promote hepatocellular carcinoma cell motility by affecting the biological functions of ITGB1 through N-glycosylation
physiological function
GnT-IVa and GnT-IVb have glycosyltransferase activity that generates the type-2 diabetes-related beta1,4-GlcNAc branch on the alpha1,3-Man arm of N-glycans
additional information
the lectin domain plays a unique and pivotal role in the regulation of GnT-IV activity
additional information
the lectin domain plays a unique and pivotal role in the regulation of GnT-IV activity
additional information
the lectin domain plays a unique and pivotal role in the regulation of GnT-IV activity
additional information
the lectin domain plays a unique and pivotal role in the regulation of GnT-IV activity
Show AA Sequence and Transmembrane Helices (1188 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
94000
recombinant HsGnT-IVa with the first 87 amino acids removed and fused with maltose-binding protein (MBP-GnT-IVa-DELTA87), SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 94000, recombinant HsGnT-IVa with the first 87 amino acids removed and fused with maltose-binding protein (MBP-GnT-IVa-DELTA87), SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
N-glycosylated enzyme. One N-glycan attached to the lectin domain, which is proximal to the ligand binding site
glycoprotein
N-glycosylated enzyme. One N-glycan attached to the lectin domain, which is proximal to the ligand binding site
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion method at 20C. Crystal structure of the C-terminal region (CBML, carbohydrate-binding module), and its complex with beta-GlcNAc at 1.97, 1.47, and 1.15 A resolution
hanging-drop vapor diffusion method at 20C. Crystal structure of the C-terminal region (CBML, carbohydrate-binding module), and its complex with beta-GlcNAc at 1.97, 1.47, and 1.15 A resolution
hanging-drop vapor diffusion method at 20C. Crystal structure of the C-terminal region (CBML, carbohydrate-binding module), and its complex with beta-GlcNAc at 1.97, 1.47, and 1.15 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F413H
no statistically significant differences in the activity toward the oligosaccharide from wild-type enzyme GnTIVb. Enhanced activity toward particular glycoprotein substrates, such as haptoglobin, alpha1 antitrypsin, and transferrin, which are the best three substrates for GnT-IVa
I456Q
no statistically significant differences in the activity toward the oligosaccharide from wild-type enzyme GnTIVb
additional information
additional information
knockdown of GnT-IVa in 1668 cells and HepG2 cells by transfection with GnT-IVa shRNA. The level of NA3Fb decreases and M8 increases in knockdown GnT-IVa/1668 cells compared with GnT-IVa/NC after 48 h transfection. The scratch healing rates of the GnT-IVa/1668 group decreases more than the GnT-IVa/NC group. High expression of GnT-IVa leads to a higher level of NA3Fb in the HCC cell surface, and the downregulation of GnT-IVa may modulate cell invasion and migration through NA3Fb glycan
additional information
-
knockdown of GnT-IVa in 1668 cells and HepG2 cells by transfection with GnT-IVa shRNA. The level of NA3Fb decreases and M8 increases in knockdown GnT-IVa/1668 cells compared with GnT-IVa/NC after 48 h transfection. The scratch healing rates of the GnT-IVa/1668 group decreases more than the GnT-IVa/NC group. High expression of GnT-IVa leads to a higher level of NA3Fb in the HCC cell surface, and the downregulation of GnT-IVa may modulate cell invasion and migration through NA3Fb glycan
additional information
establishment of a choriocarcinoma cell line with GnT-IVa overexpression (Jar-GnT4a), and examination of its malignant potential and target proteins for GnT-IVa glycosylation. GnT-IVa overexpression increases the cell migration and invasion (2.5 and 1.4fold) as well as the ability to adhere to the extracellular matrix (ECM) components, including fibronectin and collagen type I and IV. The tumour formation potential of Jar-GnT4a in mice is significantly higher than that of control, and the cumulative survival rate of mice with Jar-GnT4a is relatively lower than those with control. Immunoprecipitation studies show that beta1,4GlcNAc branches of N-glycans on integrin beta1 in choriocarcinoma cells are increased by GnT-IVa overexpression
additional information
-
establishment of a choriocarcinoma cell line with GnT-IVa overexpression (Jar-GnT4a), and examination of its malignant potential and target proteins for GnT-IVa glycosylation. GnT-IVa overexpression increases the cell migration and invasion (2.5 and 1.4fold) as well as the ability to adhere to the extracellular matrix (ECM) components, including fibronectin and collagen type I and IV. The tumour formation potential of Jar-GnT4a in mice is significantly higher than that of control, and the cumulative survival rate of mice with Jar-GnT4a is relatively lower than those with control. Immunoprecipitation studies show that beta1,4GlcNAc branches of N-glycans on integrin beta1 in choriocarcinoma cells are increased by GnT-IVa overexpression
additional information
replacement of a nonconserved amino acid in the GnT-IVb lectin domain with the corresponding residue in GnT-IVa alters the glycoprotein preference of GnT-IVb to resemble that of GnT-IVa
additional information
replacement of a nonconserved amino acid in the GnT-IVb lectin domain with the corresponding residue in GnT-IVa alters the glycoprotein preference of GnT-IVb to resemble that of GnT-IVa
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
GnT-IVb undergoes proteolysis or degradation more readily than GnT-IVa in cells
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose and Cu2+ Sepharose chromatography, followed by UDP-hexanolamine-agarose affinity chomatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Spodoptera frugiperda and Trichoplusia ni cells by using a baculovirus expression vector
-
recombinant full-length enzyme and soluble truncated form tagged with FLAG sequence at the N-terminus. expressed in COS7 cells, N-acetylglucosaminyltransferase-IVa
-
recombinant full-length enzyme and soluble truncated form tagged with FLAG sequence at the N-terminus. expressed in COS7 cells, N-acetylglucosaminyltransferase-IVb
-
the enzyme is cloned as an N-terminal truncated form that is fused with solubility-enhancing tags or signal peptides and overexpressed in Escherichia coli Rosetta (DE3). Recombinant HsGnT-IVa could be overexpressed in its highest soluble and active form when the first 87 amino acids are removed and is fused with maltose-binding protein (MBP-GnT-IVa-DELTA87). By optimizing the induction conditions, the expression level of the recombinant protein is increased to yield approximately 540 mg/l of culture after affinity purification
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
hepatitis C virus infection inhibits GLUT2 N-glycosylation on the pancreatic beta cell surface by downregulating the expression of GnT-IVa and then activates the ATP-sensitive potassium channel pathway, which ultimately leads to disturbances in insulin secretion
Mgat4a expression is induced under hypoxic conditions. Isoform GnT-IVa expression is aberrantly up-regulated in some type of tumor cells
-
Mgat4a expression levels are significantly reduced in the pancreatic beta cells of type 2 diabetes patients
-
the enzyme is upregulated in hepatocellular carcinoma tissues and positively correlates with worse outcomes in hepatocellular carcinoma patients
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
synthesis
medicine
-
enzyme activity is elevated in three choriocarcinoma cell lines compared to normal placenta. Activity in JEG-3 cells is 29 times higher than normal
medicine
-
enzyme activity in tissue from patients with extrahepatic bile duct carcinoma remains unchanged
synthesis
-
it is necessary to select appropriate host cell lines according to their glycosyltransferases activity balance to produce glycoproteins with an objective sugar chain structure. The descibed method of grouping cell lines according to their glycosyltransferases activity balance is useful to select appropriate host cells
synthesis
approach for the large-scale production of bioactive HsGnT-IVa, which can be used for in vitro synthesis and functional studies of multiantennary complex-type N-glycans
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schachter, H.; Brockhausen, I.; Hull, E.
High-performance liquid chromatography assays for N-acetylglucosaminyltransferases involved in N- and O-glycan synthesis
Methods Enzymol.
179
351-397
1989
Gallus gallus
brenda
Gleeson, P.A.; Schachter, H.
Control of glycoprotein synthesis
J. Biol. Chem.
258
6162-6173
1983
Gallus gallus
brenda
Taniguchi, N.; Nishikawa, A.; Fujii, S.; Gu, J.
Glycosyltransferase assays using pyridylaminated acceptors: N-acetylglucosaminyltransferase III, IV, and V
Methods Enzymol.
179
397-408
1989
Rattus norvegicus
brenda
Oguri, S.; Minowa, M.T.; Ihara, Y.; Taniguchi, N.; Ikenaga, H.; Takeuchi, M.
Purification and characterization of UDP-N-acetylglucosamine: alpha1,3-D-mannoside beta1,4-N-acetylglucosaminyltransferase (N-acetylglucosaminyltransferase-IV) from bovine small intestine
J. Biol. Chem.
272
22721-22727
1997
Bos taurus (O77836)
brenda
Zhu, T.Y.; Chen, H.L.; Gu, J.X.; Zhang, Y.F.; Zhang, Y.K.; Zhang, R.A.
Changes in N-acetylglucosaminyltransferase III, IV, and V in renal cell carcinoma
J. Cancer Res. Clin. Oncol.
123
296-299
1997
Homo sapiens
brenda
Minowa, M.T.; Oguri, S.; Yoshida, A.; Hara, T.; Iwamatsu, A.; Ikenaga, H.; Takeuchi, M.
cDNA cloning and expression of bovine UDP-N-acetylglucosamine: alpha1,3-D-mannoside beta1,4-N-acetylglucosaminyltransferase IV
J. Biol. Chem.
273
11556-11562
1998
Bos taurus (O77836), Bos taurus
brenda
Yoshida, A.; Minowa, M.T.; Takamatsu, S.; Hara, T.; Ikenaga, H.; Takeuchi, M.
A novel second isoenzyme of the human UDP-N-acetylglucosamine:alpha1,3-D-mannoside beta1,4-N-acetylglucosaminyltransferase family: cDNA cloning, expression, and chromosomal assignment
Glycoconjugate J.
15
1115-1123
1998
Homo sapiens (Q9UQ53), Homo sapiens
brenda
Nan, B.C.; Shao, D.M.; Chen, H.L.; Huang, Y.; Gu, J.X.; Zhang, Y.B.; Wu, Z.G.
Alteration of N-acetylglucosaminyltransferases in pancreatic carcinoma
Glycoconjugate J.
15
1033-1037
1998
Homo sapiens
brenda
Yoshida, A.; Minowa, M.T.; Takamatsu, S.; Hara, T.; Oguri, S.; Ikenaga, H.; Takeuchi, M.
Tissue specific expression and chromosomal mapping of a human UDP-N-acetylglucosamine:alpha1,3-D-mannoside beta1,4-N-acetylglucosaminyltransferase
Glycobiology
9
303-310
1999
Homo sapiens (Q9UM21), Homo sapiens
brenda
Takamatsu, S.; Oguri, S.; Minowa, M.T.; Yoshida, A.; Nakamura, K.; Takeuchi, M.; Kobata, A.
Unusually high expression of N-acetylglucosaminyltransferase-IVa in human choriocarcinoma cell lines: a possible enzymatic basis of the formation of abnormal biantennary sugar chain
Cancer Res.
59
3949-3953
1999
Homo sapiens
brenda
Takamatsu, S.; Inoue, N.; Katsumata, T.; Nakamura, K.; Fujibayashi, Y.; Takeuchi, M.
The relationship between the branch-forming glycosyltransferases and cell surface sugar chain structures
Biochemistry
44
6343-6349
2005
Homo sapiens
brenda
Jin, X.L.; Liu, H.B.; Zhang, Y.; Wang, B.S.; Chen, H.L.
Alteration in N -acetylglucosaminyltransferase activities and glycan structure in tissue and bile glycoproteins from extrahepatic bile duct carcinoma
Glycoconj. J.
20
399-406
2004
Homo sapiens
brenda
Takamatsu, S.; Katsumata, T.; Inoue, N.; Watanabe, T.; Fujibayashi, Y.; Takeuchi, M.
Abnormal biantennary sugar chains are expressed in human chorionic gonadotropin produced in the choriocarcinoma cell line, JEG-3
Glycoconj. J.
20
473-481
2004
Homo sapiens
brenda
Ide, Y.; Miyoshi, E.; Nakagawa, T.; Gu, J.; Tanemura, M.; Nishida, T.; Ito, T.; Yamamoto, H.; Kozutsumi, Y.; Taniguchi, N.
Aberrant expression of N-acetylglucosaminyltransferase-IVa and IVb (GnT-IVa and b) in pancreatic cancer
Biochem. Biophys. Res. Commun.
341
478-482
2006
Homo sapiens (Q9UQ53), Homo sapiens (Q9UM21)
brenda
Oguri, S.; Yoshida, A.; Minowa, M.T.; Takeuchi, M.
Kinetic properties and substrate specificities of two recombinant human N-acetylglucosaminyltransferase-IV isozymes
Glycoconj. J.
23
473-480
2006
Homo sapiens
brenda
Kim, N.Y.; Kim, H.G.; Kim, Y.H.; Chung, I.S.; Yang, J.M.
Expression and characterization of human N-acetylglucosaminyltransferases and alpha2,3-sialyltransferase in insect cells for in vitro glycosylation of recombinant erythropoietin
J. Microbiol. Biotechnol.
18
383-391
2008
Homo sapiens
brenda
Kudo, T.; Nakagawa, H.; Takahashi, M.; Hamaguchi, J.; Kamiyama, N.; Yokoo, H.; Nakanishi, K.; Nakagawa, T.; Kamiyama, T.; Deguchi, K.; Nishimura, S.; Todo, S.
N-glycan alterations are associated with drug resistance in human hepatocellular carcinoma
Mol. Cancer
6
32
2007
Homo sapiens (Q9UQ53), Homo sapiens (Q9UM21), Homo sapiens
brenda
Takamatsu, S.; Antonopoulos, A.; Ohtsubo, K.; Ditto, D.; Chiba, Y.; Le, D.T.; Morris, H.R.; Haslam, S.M.; Dell, A.; Marth, J.D.; Taniguchi, N.
Physiological and glycomic characterization of N-acetylglucosaminyltransferase-IVa and -IVb double deficient mice
Glycobiology
20
485-497
2010
Mus musculus
brenda
Fan, J.; Wang, S.; Yu, S.; He, J.; Zheng, W.; Zhang, J.
N-acetylglucosaminyltransferase IVa regulates metastatic potential of mouse hepatocarcinoma cells through glycosylation of CD147
Glycoconj. J.
29
323-334
2012
Mus musculus
brenda
Nagels, B.; Van Damme, E.J.; Pabst, M.; Callewaert, N.; Weterings, K.
Production of complex multiantennary N-glycans in Nicotiana benthamiana plants
Plant Physiol.
155
1103-1112
2011
Homo sapiens
brenda
Ohtsubo, K.
Biological significance of N-acetylglucosaminyltransferase-IV-mediated protein glycosylation on the homeostasis of cellular physiological functions
Trends Glycosci. Glycotechnol.
23
103-105
2011
Homo sapiens, Bos taurus
-
brenda
Nie, H.; Liu, X.; Zhang, Y.; Li, T.; Zhan, C.; Huo, W.; He, A.; Yao, Y.; Jin, Y.; Qu, Y.; Sun, X.L.; Li, Y.
Specific N-glycans of hepatocellular carcinoma cell surface and the abnormal increase of core-alpha-1,6-fucosylated triantennary Glycan via N-acetylglucosaminyltransferases-IVa regulation
Sci. Rep.
5
16007
2015
Homo sapiens (Q9UM21), Homo sapiens
brenda
Nishino, K.; Yamamoto, E.; Niimi, K.; Sekiya, Y.; Yamashita, Y.; Kikkawa, F.
N-acetylglucosaminyltransferase IVa promotes invasion of choriocarcinoma
Oncol. Rep.
38
440-448
2017
Homo sapiens (Q9UM21), Homo sapiens
brenda
Yang, D.; Han, F.; Cai, J.; Sun, H.; Wang, F.; Jiang, M.; Zhang, M.; Yuan, M.; Zhou, W.; Li, H.; Yang, L.; Bai, Y.; Xiao, L.; Dong, H.; Cheng, Q.; Mao, H.; Zhou, L.; Wang, R.; Li, Y.; Nie, H.
N-glycosylation by N-acetylglucosaminyltransferase IVa enhances the interaction of integrin beta1 with vimentin and promotes hepatocellular carcinoma cell motility
Biochim. Biophys. Acta Mol. Cell Res.
1870
119513
2023
Homo sapiens (Q9UM21), Mus musculus (Q812G0)
brenda
Osada, N.; Nagae, M.; Yamasaki, T.; Harduin-Lepers, A.; Kizuka, Y.
Regulation of human GnT-IV family activity by the lectin domain
Carbohydr. Res.
545
109285
2024
Homo sapiens (Q9UQ53), Homo sapiens (Q9UM21), Mus musculus (Q812G0), Mus musculus (Q812F8)
brenda
Niu, B.; Ma, L.; Yao, L.; Zhang, Y.; Su, H.
HCV affects KATP channels through GnT-IVa-mediated N-glycosylation of GLUT2 on the surface of pancreatic beta-cells leading to impaired insulin secretion
Endocrine
84
427-440
2024
Rattus norvegicus (Q5M854)
brenda
Peng, S.L.; Ding, Y.; Xiang, M.H.; Chen, K.; Gao, X.D.; Wang, N.
Enhanced soluble expression and characterization of human N-acetylglucosaminyltransferase IVa in Escherichia coli
Enzyme Microb. Technol.
181
110524
2024
Homo sapiens (Q9UM21)
brenda
Oka, N.; Mori, S.; Ikegaya, M.; Park, E.Y.; Miyazaki, T.
Crystal structure and sugar-binding ability of the C-terminal domain of N-acetylglucosaminyltransferase IV establish a new carbohydrate-binding module family
Glycobiology
32
1153-1163
2022
Homo sapiens (Q9UM21), Bombyx mandarina (A0A6J2K041)
brenda
Osada, N.; Nagae, M.; Nakano, M.; Hirata, T.; Kizuka, Y.
Examination of differential glycoprotein preferences of N-acetylglucosaminyltransferase-IV isozymes a and b
J. Biol. Chem.
298
102400
2022
Homo sapiens (Q9UQ53), Homo sapiens (Q9UM21)
brenda
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