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2.4.1.37: fucosylgalactoside 3-alpha-galactosyltransferase

This is an abbreviated version!
For detailed information about fucosylgalactoside 3-alpha-galactosyltransferase, go to the full flat file.

Word Map on EC 2.4.1.37

Reaction

UDP-alpha-D-galactose
+
alpha-L-fucosyl-(1->2)-D-galactosyl-R
=
UDP
+
alpha-D-galactosyl-(1->3)-[alpha-L-fucosyl(1->2)]-D-galactosyl-R

Synonyms

ABO(H) blood group B alpha-(1->3)-galactosyltransferase, ABO(H) blood group B alpha-1,3-galactosyltransferase, ABO(H) blood group B glycosyltransferase, ABO(H) blood-group glycosyltransferase B, alpha(1-3)galactosyltransferase, alpha-(1,3)-galactosyltransferase, alpha-(1-3)-galactosyltransferase, alpha-(1->3)-galactosyltransferase, alphaGal-T1, B glycosyltransferase, B transferase, blood group alpha-(1-3)-galactosyltransferase, blood group B alpha-(1,3)-galactosyltransferase, blood group B galactosyltransferase, blood group B glycosyltransferase, blood group B glycosyltransferase GTB, blood group B-glycosyltransferase, blood-group substance B-dependent galactosyltransferase, cis-AB-transferase, glycoprotein-fucosylgalactoside alpha-galactosyltransferase, glycosyltransferases B, GTB, histo-blood group ABO system transferase, histo-blood group B enzyme, histo-blood group B transferase, histo-blood substance B-dependent galactosyltransferase, More, UDP-galactose:fucoside alpha1,3-galactosyltransferase, UDP-galactose:O-alpha-L-fucosyl(1-2)D-galactose alpha-D-galactosyltransferase, UDPgalactose:glycoprotein-alpha-L-fucosyl-(1,2)-D-galactose 3-alpha-D-galactosyltransferase, [blood group substance] alpha-galactosyltransferase

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.37 fucosylgalactoside 3-alpha-galactosyltransferase

Engineering

Engineering on EC 2.4.1.37 - fucosylgalactoside 3-alpha-galactosyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A268T
C209A
site-directed mutagenesis, mutant structure determination
C80S/C196S
-
both the double and triple mutants show differing levels of disorder depending on their liganded state, with the level of disorder increasing when substrates are bound.The double mutant shows disorder over residues 177-180 in the unliganded and H-antigen bound forms, with disorder increasing to residues 176-185 for the UDP-, UDP + H-, and UDP-alpha-D-galactose + 3-deoxy-Gal inactive acceptor analog-bound structures. The double mutant has a reduction in Km for both donor and acceptor substrates. Mutation shows little effect over kcat
C80S/C196S/C209S
-
both the double and triple mutants show differing levels of disorder depending on their liganded state, with the level of disorder increasing when substrates are bound.The unliganded triple mutant shows a nearly complete internal loop, with residues 176-181 disordered for the H-antigen-bound structure and 177-179 disordered for the UDP-bound structure. The UDP + H- and UDPGal + 3-deoxy-Gal inactive acceptor analog-bound structures of the triple mutant show an internal loop completely disordered over residues 176-184. The triple Cys-to-Ser mutant has an acceptor Km elevated approximately 5times over wild type, while the donor Km has doubled. Mutation shows little effect over kcat
D262N
D302A
almost complete loss of activity
D302A/D316A
strong decrease in kcat value
D302C
kcat value is 9% that of wild-type GTB
D302E
kcat value is 47% that of wild-type GTB
D302E/D316E
50% decrease in kcat value
D302L
almost complete loss of activity
DELTA68-354
-
construct in which the N-terminal transmembrane domain is deleted. Deletion results in a more crystallizable protein
E303A
residue E303 plays a critical role in maintaining the stability of a strained double-turn in the active site through several hydrogen bonds
E303C
residue E303 plays a critical role in maintaining the stability of a strained double-turn in the active site through several hydrogen bonds. Mutant retains significant activity despite disrupted active site architecture
E303D
residue E303 plays a critical role in maintaining the stability of a strained double-turn in the active site through several hydrogen bonds. Mutant retains significant activity despite disrupted active site architecture
E303Q
residue E303 plays a critical role in maintaining the stability of a strained double-turn in the active site through several hydrogen bonds. Mutant maintains active site architecture but exhibits zero activity
F216I
I192T
M186V
-
site-directed mutagenesis, mutation is a naturally occuring polymorphism, amino-acid substitution in the disordered loop of the enzyme causes a weak B phenotype of erythrocytes, mutant enzyme shows reduced activity compared to the wild-type enzyme
M189V
M214G
-
saturation mutagenesis of GTB enzyme at M214 leads to a two-fold higher kcat for UDP-GalNAc and specific activity of the mutant compared to the wild-type GTB
M214R
mutation is adjacent to the 211DVD213 motif. 1200fold decrease in kcat compared with wild type enzyme. The crystal structure of M214R shows that DVD motif coordination to Mn2+ is disrupted by Arg214 causing displacement of the metal by a water molecule. Individuals with the M214R mutation show the Bel variant expressing very low levels of B antigens
M214S
-
saturation mutagenesis of GTB enzyme at M214 leads to a two-fold higher kcat for UDP-GalNAc and specific activity of the mutant compared to the wild-type GTB
M214T
mutation is adjacent to the 211DVD213 motif. The crystal structure of the M214T mutant shows no change in DVD motif coordination to Mn2+. Instead a critical residue, Met266, which is responsible for determining donor specificity, has adopted alternate conformations. The conformation with the highest occupancy opens up the active site to accommodate the larger A-specific donor, UDP-GalNAc, accounting for the dual specificity. Individuals with M214T mutation give rise to AweakB phenotype
M214V
mutation is adjacent to the 211DVD213 motif. Individuals with M214T mutation give rise to AweakB phenotype
P234S
dramatic and complete reversal of donor specificity, it preferentially utilizes UDP-GalNac for transfer
R188H
site-directed mutagenesis, the mutant shows affected substrate binding
R188K
R188S
S185C
mutant enzyme exhibits 4.8fold elevations in kcat/Km for UDP-glucose relative to that of wild-type enzyme
S185D
activity with UDP-galactose is 0.09% of wild-type activity
S185E
activity with UDP-galactose is 0.04% of wild-type activity
S185N
mutant enzyme exhibits 4.3fold elevations in kcat/Km for UDP-glucose relative to that of wild-type enzyme
additional information