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Literature summary for 2.4.1.155 extracted from

  • Pinho, S.S.; Figueiredo, J.; Cabral, J.; Carvalho, S.; Dourado, J.; Magalhaes, A.; Gaertner, F.; Mendonca, A.M.; Isaji, T.; Gu, J.; Carneiro, F.; Seruca, R.; Taniguchi, N.; Reis, C.A.
    E-cadherin and adherens-junctions stability in gastric carcinoma: Functional implications of glycosyltransferases involving N-glycan branching biosynthesis, N-acetylglucosaminyltransferases III and V (2012), Biochim. Biophys. Acta, 1830, 2690-2700.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene MGAT5, quantitative real-time PCR enzyme expression analysis Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information GnT-V overexpression induces an aberrant E-cadherin cellular localization and alters cell morphology, GnT-V increases the stability of the cadherin/catenin complex, GnT-V leads to a reduced intercellular adhesion of gastric cells, phenotype, overview Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-N-acetyl-D-glucosamine + 6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R Homo sapiens
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UDP + 6-(2,6-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q09328 gene MGAT5
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Source Tissue

Source Tissue Comment Organism Textmining
epithelium
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Homo sapiens
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gastric carcinoma cell
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Homo sapiens
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MKN-45 cell
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Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-N-acetyl-D-glucosamine + 6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
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Homo sapiens UDP + 6-(2,6-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
-
?

Synonyms

Synonyms Comment Organism
GnT-V
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Homo sapiens
N-acetylglucosaminyltransferase V
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Homo sapiens

General Information

General Information Comment Organism
malfunction GnT-V overexpression induces an aberrant E-cadherin cellular localization and alters cell morphology, fibroblastoid cells exhibit a remarkable decrease of E-cadherin membranar expression with punctual E-cadherin staining in focal areas of cell-cell contacts Homo sapiens
metabolism existence of a bi-directional cross-talk between E-cadherin and two major N-glycan processing enzymes, N-acetylglucosaminyltransferase-III or -V (GnT-III or GnT-V). Molecular mechanisms underlying E-cadherin regulation in gastric cancer, overview Homo sapiens
physiological function GnT-V promotes the destabilization of E-cadherin at the cell membrane leading to its mislocalization and unstable adherens-junctions with impairment of cell–cell adhesion. Role pf the enzyme GnT-V in E-cadherin-mediated tumor invasion. GnT-V catalyzes the addition of ?1,6 GlcNAc branching N-glycans and is associated to increased metastasis. E-cadherin is specifically modified with bisecting GlcNAc or beta1,6 GlcNAc branched structures Homo sapiens