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Literature summary extracted from

  • Miyazaki, T.; Miyashita, R.; Mori, S.; Kato, T.; Park, E.Y.
    Expression and characterization of silkworm Bombyx mori beta-1,2-N-acetylglucosaminyltransferase II, a key enzyme for complex-type N-glycan biosynthesis (2019), J. Biosci. Bioeng., 127, 273-280 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.143 gene GnTII, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, functional expression of the enzyme using a silkworm-based Bombyx mori nucleopolyhedrovirus bacmid expression system, the enzyme is secreted. The recombinant enzyme exhibits similar pH and temperature dependency and the same substrate specificity as human GnTII expressed by the same system, but deglycosylation with peptide:N-glycanase F does not affect its enzymatic activity. Construction of a vector including the N-terminally FLAG (DYKDDDDK)-tagged lumenal region (Leu27eAla498) including the stem domain and the catalytic domain of BmGnTII together with a signal peptide sequence from bombyxin and transformed into Escherichia coli BmDH10Bac-CP-/Chi- competent cells, which contain the cysteine protease- and chitinase-deficient BmNPV bacmid. RT-PCR expression analysis. The cDNA templates are synthesized from total RNAs extracted from whole bodies of first to fifth-instar larvae and pupa and tissues of fifth-instar larvae. Tissues used are as follows: fat body, midgut, silk gland, epidermis, and Malpighian tubule. To produce the soluble form of BmGnTII n hemolymph, chitosan/BmNPV bacmid nanocomplexes are prepared and then injected into fifth-instar silkworm larvae. The bacmid-injected larvae are reared on an artificial diet Bombyx mori

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.143 additional information construction of a vector including the N-terminally FLAG (DYKDDDDK)-tagged lumenal region (Leu27eAla498) including the stem domain and the catalytic domain of BmGnTII together with a signal peptide sequence from bombyxin and transformed into Escherichia coli BmDH10Bac-CP--Chi- competent cells, which contain the cysteine protease- and chitinase-deficient BmNPV bacmid. RT-PCR expression analysis. The cDNA templates are synthesized from total RNAs extracted from whole bodies of first to fifth-instar larvae and pupa and tissues of fifth-instar larvae. Tissues used are as follows: fat body, midgut, silk gland, epidermis, and Malpighian tubule. To produce the soluble form of BmGnTII n hemolymph, chitosan/BmNPV bacmid nanocomplexes are prepared and then injected into fifth-instar silkworm larvae. The bacmid-injected larvae are reared on an artificial diet Bombyx mori

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.1.143 Mn2+ required Bombyx mori

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.143 alpha-D-Man-(1->6)-[beta-D-GlcNAc(1->2)-alpha-D-Man(1->3)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc + UDP-GlcNAc Bombyx mori i.e. pyridylaminated MGn glycan, an intermediate during N-glycan processing ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.143 Bombyx mori A0A451FEC8
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.143 epidermis
-
 Bombyx mori
-
2.4.1.143 fat body
-
 Bombyx mori
-
2.4.1.143 malpighian tubule
-
 Bombyx mori
-
2.4.1.143 midgut
-
 Bombyx mori
-
2.4.1.143 silk gland
-
 Bombyx mori
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.143 alpha-D-Man-(1->6)-[beta-D-GlcNAc(1->2)-alpha-D-Man(1->3)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc + UDP-GlcNAc i.e. pyridylaminated MGn glycan, an intermediate during N-glycan processing Bombyx mori ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.143 beta-1,2-N-acetylglucosaminyltransferase II
-
 Bombyx mori
2.4.1.143 BmGnTII
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 Bombyx mori
2.4.1.143 GnTII
-
 Bombyx mori
2.4.1.143 Mgat2 UniProt Bombyx mori

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.143 37
-
 assay at Bombyx mori

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.143 6.5
-
 assay at Bombyx mori

General Information

EC Number General Information Comment Organism
2.4.1.143 evolution compared with the structure of human GnTII, the amino acid residues involved in catalytic activity and substrate recognition are almost fully conserved in Bombyx mori GnTII, which is consistent with its enzymatic properties Bombyx mori
2.4.1.143 metabolism beta-1,2-N-acetylglucosaminyltransferase II is a key enzyme for complex-type N-glycan biosynthesis. Both insect and mammalian cells produce Man(alpha1->6)[GlcNAc(beta1->2)Man(alpha1->3)]Man(beta1->4)GlcNAc(beta1->4)GlcNAc (MGn) glycan as an intermediate during N-glycan processing. In insect cells, beta-N-acetylglucosaminidase (fused lobes, FDL) removes a GlcNAc residue of the alpha1-3 arm of MGn glycan to produce Man(alpha1->6)[Man(alpha1->3)]ManGlcNAc2 (MM), a core structure from paucimannose-type N-glycans Bombyx mori
2.4.1.143 physiological function beta-1,2-N-acetylglucosaminyltransferase II (GnTII) catalyzes the transfer of GlcNAc from a UDP-GlcNAc donor to the alpha1-6 arm of MGn glycan to produce biantennary complex-type glycans in mammalian cells Bombyx mori