Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.4.1.133 extracted from

  • Siegbahn, A.; Thorsheim, K.; Stahle, J.; Manner, S.; Hamark, C.; Persson, A.; Tykesson, E.; Mani, K.; Westergren-Thorsson, G.; Widmalm, G.; Ellervik, U.
    Exploration of the active site of beta4GalT7: modifications of the aglycon of aromatic xylosides (2015), Org. Biomol. Chem., 13, 3351-3362.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics, molecular docking simulations of the Michaelis complex Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens some beta-D-xylosides, such as 2-naphthyl beta-D-xylopyranoside, can induce glycosaminoglycan synthesis by serving as acceptor substrates for beta4GalT7 and by that also compete with the glycosaminoglycan synthesis on core proteins ?
-
?
UDP-alpha-D-galactose + 2-naphthyl beta-D-xylopyranoside Homo sapiens
-
UDP + 4-beta-D-galactosyl-2-naphthyl-beta-D-xylopyranoside
-
?
UDP-alpha-D-galactose + O-beta-D-xylosyl-[protein] Homo sapiens
-
UDP + 4-beta-D-galactosyl-O-beta-D-xylosyl-[protein]
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9UBV7 gene B4GALT7
-

Source Tissue

Source Tissue Comment Organism Textmining
HCC-70 cell
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information some beta-D-xylosides, such as 2-naphthyl beta-D-xylopyranoside, can induce glycosaminoglycan synthesis by serving as acceptor substrates for beta4GalT7 and by that also compete with the glycosaminoglycan synthesis on core proteins Homo sapiens ?
-
?
additional information structure-activity relationships for beta4GalT7 and xylosides with modifications of the aromatic aglycon, using enzymatic assays, cell studies, and molecular docking simulations, show that the aglycons reside on the outside of the active site of the enzyme and that quite bulky aglycons are accepted. Increased galactosylation with increased linker length is observed, substrate specificity with glycosides, detailed overview. The galactosylation is influenced by the identity and position of substituents in the aromatic framework, and generally, only xylosides with beta-glycosidic linkages function as good substrates for the enzyme. The galactosylation ability of a xyloside is increased by replacing the anomeric oxygen with sulfur, but decreased by replacing it with carbon. Enzyme reaction kinetics of galactosylation are dependent on subtle differences in orientation of the xylose moiety Homo sapiens ?
-
?
UDP-alpha-D-galactose + 2-naphthyl beta-D-xylopyranoside
-
Homo sapiens UDP + 4-beta-D-galactosyl-2-naphthyl-beta-D-xylopyranoside
-
?
UDP-alpha-D-galactose + O-beta-D-xylosyl-[protein]
-
Homo sapiens UDP + 4-beta-D-galactosyl-O-beta-D-xylosyl-[protein]
-
?

Synonyms

Synonyms Comment Organism
beta4GalT7
-
Homo sapiens

General Information

General Information Comment Organism
additional information molecular docking of substrate-bound enzyme using structures PDB ID 4LW6 and PDB ID 4M4K Homo sapiens
physiological function the galactosyltransferase beta4GalT7 is involved in the biosynthesis of glycosaminoglycan chains, initiated by xylosylation of the core protein followed by galactosylation by the enzyme Homo sapiens