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Literature summary extracted from

  • Ramakrishnan, B.; Qasba, P.K.
    Crystal structure of lactose synthase reveals a large conformational change in its catalytic component, the beta1,4-galactosyltransferase-I (2001), J. Mol. Biol., 310, 205-218.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.1.22 catalytic domain of recombinant bovine beta4Gal-T1 from residues 130 to 402, d129 beta4Gal-T1, 33000 Da, and mouse recombinant alpha-lactalbumin. Crystal structure of enzyme bound with various substrates Mus musculus
2.4.1.22 catalytic domain of recombinant bovine beta4Gal-T1 from residues 130 to 402, d129 beta4Gal-T1, 33000 Da, and mouse recombinant alpha-lactalbumin. Crystal structure of enzyme bound with various substrates Bos taurus
2.4.1.38 recombinant enzyme, crystal structure of lactose synthase reveals a large conformational change in its catalytic component, the beta1,4-galactosyltransferase-I Bos taurus
2.4.1.90 recombinant enzyme, crystal structure of lactose synthase reveals a large conformational change in its catalytic component, the beta1,4-galactosyltransferase-I Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.22 Bos taurus
-
 catalytic domain of recombinant bovine beta4Gal-T1 from residues 130 to 402, d129 beta4Gal-T1, 33000 Da, and mouse recombinant alpha-lactalbumin
-
2.4.1.22 Mus musculus
-
-
-
2.4.1.38 Bos taurus
-
-
-
2.4.1.90 Bos taurus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.22 additional information upon substrate binding to beta4Gal-T1, a large conformational change occurs in the region comprising residues 345 to 365. The role of alpha-lactalbumin is to hold glucose by hydrogen bonding with the O-1 hydroxyl group in the acceptor-binding site on beta4Gal-T1, while the N-acetyl group-binding pocket in beta4Gal-T1 adjusts to maximize the interactions with the glucose molecule Mus musculus ?
-
 ?
2.4.1.22 additional information upon substrate binding to beta4Gal-T1, a large conformational change occurs in the region comprising residues 345 to 365. The role of alpha-lactalbumin is to hold glucose by hydrogen bonding with the O-1 hydroxyl group in the acceptor-binding site on beta4Gal-T1, while the N-acetyl group-binding pocket in beta4Gal-T1 adjusts to maximize the interactions with the glucose molecule Bos taurus ?
-
 ?
2.4.1.22 UDPgalactose + D-glucose
-
 Mus musculus lactose + UDP
-
 ?
2.4.1.22 UDPgalactose + D-glucose
-
 Bos taurus lactose + UDP
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.1.22 More
-
 Bos taurus
2.4.1.22 More the enzyme is 1.1 complex of a catalytic component beta1,4-galactosyltransferase (beta4gal-T1) and a regulatory component, alpha-lactalbumin Mus musculus