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

BRENDA support

Literature summary for 2.4.1.90 extracted from

  • Ramakrishnan, B.; Boeggeman, E.; Ramasamy, V.; Qasba, P.K.
    Structure and catalytic cycle of beta-1,4-galactosyltransferase (2004), Curr. Opin. Struct. Biol., 14, 593-600.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme in complex with Mn2+, UDP-GalNAc, glucose, and alpha-lactalbumin, X-ray diffraction structure determination and analysis at 2.0 A resolution Homo sapiens

Protein Variants

Protein Variants Comment Organism
M344H mutant prefers Mg2+ instead of Mn2+ which is preferred by the wild-type enzyme, with Mn2+ the mutant is arrested in the closed inactive conformation Bos taurus
Y289I mutant shows high activity with UDP-GalNAc in contrary to the wild-type enzyme Bos taurus
Y289L mutant shows high activity with UDP-GalNAc in contrary to the wild-type enzyme Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
Golgi apparatus
-
Homo sapiens 5794
-
Golgi apparatus
-
Bos taurus 5794
-
membrane type II membrane-bound protein Homo sapiens 16020
-
membrane type II membrane-bound protein Bos taurus 16020
-
additional information enzyme possesses a membrane-spanning domain, a cytoplasmic domain, a stem region, and the catalytic domain that faces the lumen Homo sapiens
-
-
additional information enzyme possesses a membrane-spanning domain, a cytoplasmic domain, a stem region, and the catalytic domain that faces the lumen Bos taurus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ required, binding site structure involving Met344 and Asp254, mechanism overview, binding results in conformational changes in the catalytic domain Bos taurus
Mn2+ required, binding site structure, binding results in conformational changes in the catalytic domain Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-galactose + N-acetyl-D-glucosamine Homo sapiens
-
UDP + N-acetyllactosamine
-
?
UDP-galactose + N-acetyl-D-glucosamine Bos taurus
-
UDP + N-acetyllactosamine
-
?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Homo sapiens
-
-
-

Reaction

Reaction Comment Organism Reaction ID
UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine sequential ordered catalytic mechanism, enzyme undergoes critical conformational changes upon substrate binding from an open, conf-I, to a closed conformation, conf-II, involving 2 flexible loops, a small and a long one, catalytic site structure, Tyr286 determines the specificity for UDP-Gal Homo sapiens
UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine sequential ordered catalytic mechanism, enzyme undergoes critical conformational changes upon substrate binding from an open, conf-I, to a closed conformation, conf-II, involving 2 flexible loops, a small and a long one, with Trp314 of the small loop being critical for the change interacting with both substrates, catalytic site structure, Tyr289 determines the specificity for UDP-Gal, the conformational changes create the oligosaccharide-acceptor substrate binding site Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
mammary gland
-
Homo sapiens
-
mammary gland lactating Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme interacts with alpha-lactalbumin to form the lactose synthase enzyme complex, structural basis for catalytic mechanism, overview Bos taurus ?
-
?
additional information UDP-glucose and UDP-N-acetylgalactosamine are poor substrates, the latter due to Tyr286 which is a sterical hindrance and traps hydrolyzed GalNAc in the oxocarbenium-ion-like state, enzyme interacts with alpha-lactalbumin to form the lactose synthase enzyme complex Homo sapiens ?
-
?
UDP-galactose + N-acetyl-D-glucosamine
-
Homo sapiens UDP + N-acetyllactosamine
-
?
UDP-galactose + N-acetyl-D-glucosamine
-
Bos taurus UDP + N-acetyllactosamine
-
?
UDP-galactose + N-acetyl-D-glucosamine enzyme is highly specific for UDP-galactose as donor substrate Homo sapiens UDP + N-acetyllactosamine
-
?
UDP-galactose + N-acetyl-D-glucosamine enzyme is highly specific for UDP-galactose as donor substrate, 100fold less active with UDP-glucose Bos taurus UDP + N-acetyllactosamine
-
?

Synonyms

Synonyms Comment Organism
beta-1,4-galactosyltransferase-1
-
Homo sapiens
beta-1,4-galactosyltransferase-1
-
Bos taurus
beta4Gal-T1
-
Homo sapiens
beta4Gal-T1
-
Bos taurus