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Literature summary for 2.4.1.87 extracted from

  • Ardevol, A.; Rovira, C.
    Reaction mechanisms in carbohydrate-active enzymes: glycoside hydrolases and glycosyltransferases. Insights from ab initio quantum mechanics/molecular mechanics dynamic simulations (2015), J. Am. Chem. Soc., 137, 7528-7547.
    View publication on PubMed
Search for more literature for 2.4.1.87

Crystallization (Commentary)

Crystallization (Comment) Organism
structure analysis of the enzyme in ternary complex with substrate UDP-2F-Gal, crystal structure fold-type A, PDB ID 2VFZ Bos taurus
structure analysis of the enzyme in ternary complex with substrates UDP and lactose, crystal structure fold-type A, PDB ID 1GWF Micrococcus luteus

Organism

Organism UniProt Comment Textmining
Bos taurus P14769
-
-
Micrococcus luteus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-galactose + lactose
-
 Micrococcus luteus UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-D-glucose
-
 ?
UDP-galactose + lactose
-
 Bos taurus UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-D-glucose
-
 ?

Synonyms

Synonyms Comment Organism
alpha3-galactosyltransferase
-
 Micrococcus luteus
alpha3-galactosyltransferase
-
 Bos taurus
alpha3GalT
-
 Micrococcus luteus
alpha3GalT
-
 Bos taurus

General Information

General Information Comment Organism
evolution the enzyme is a family 6 glycosyltransferase Micrococcus luteus
evolution the enzyme is a family 6 glycosyltransferase Bos taurus
additional information the N-terminal loop is folded when the acceptor substrate is bound in the active site, substrate binding structure and analysis using ab initio quantum mechanics/molecular mechanics dynamic simulations, overview Micrococcus luteus
additional information the N-terminal loop is folded when the acceptor substrate is bound in the active site, substrate binding structure and analysis using ab initio quantum mechanics/molecular mechanics dynamic simulations, overview Bos taurus