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UDP-Gal + L-fucosyl-alpha-1,2-beta-galactosyl-O(CH2)7CH3
?
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + 2'-fucosyllactose
UDP + N-acetyl-alpha-D-galactosaminyl-(1,3)-[2'-fucosyllactose]
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
UDP + alpha-D-GalNAc-(1->3)-[alpha-Fuc-(1->2)]-beta-D-Gal-(CH2)7CH3
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
UDP + N-acetyl-alpha-D-galactosaminyl-(1->3)-[alpha-Fuc-(1->2)]-beta-D-Gal-(CH2)7CH3
-
-
-
?
UDP-N-acetyl-D-galactosamine + 2'-fucosyllactose
UDP + N-acetyl-alpha-D-galactosaminyl-(1->3)-[alpha-L-fucosyl-(1->2)]-beta-D-galactosyl-(1->4)-beta-D-glucose
-
-
-
?
UDP-N-acetyl-D-galactosamine + 2'-fucosyllactose
UDP + N-acetyl-alpha-D-galactosaminyl-2'-fucosyllactose
UDP-N-acetyl-D-galactosamine + alpha-L-fucosyl-1-2-D-galactosyl-O-R
UDP + N-acetyl-alpha-D-galactosaminyl-1,3-[alpha-L-fucosyl-1-2]-D-galactosyl-O-R
UDP-N-acetyl-D-galactosamine + alpha-L-Fucp-(1,2)-beta-D-Galp-(1,3)-beta-DGlcNAcp-O(CH2)7CH3
?
41% of the activity with alpha-L-Fucp-(1,2)-beta-D-Galp-O(CH2)7CH3
-
-
?
UDP-N-acetyl-D-galactosamine + alpha-L-Fucp-(1,2)-beta-D-Galp-(1,4)-beta-D-GlcNAcp-O-(CH2)8CO2CH3
?
79% of the activity with alpha-L-Fucp-(1,2)-beta-D-Galp-O(CH2)7CH3
-
-
?
UDP-N-acetyl-D-galactosamine + alpha-L-Fucp-(1,2)-beta-D-Galp-O(CH2)7CH3
UDP + alpha-D-GalNAc-(1,3)-[alpha-(Fucp-(1,2)])-beta-D-Galp-O(CH2)7CH3
-
-
-
?
UDP-N-acetyl-D-galactosamine + asialo-porcine submaxillary mucin of A-negative blood-type
UDP + N-acetyl-alpha-D-galactosaminyl-1,3-[asialo-porcine submaxillary mucin of A-negative blood-type]
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein N-acetyl-alpha-D-galactosaminyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
UDP-N-acetyl-D-galactosamine + glycoprotein-alpha-L-fucosyl-(1,2)-D-galactose
UDP + glycoprotein-N-acetyl-alpha-D-galactosaminyl-(1,3)-[alpha-L-fucosyl-(1,2)]-D-galactose
UDP-N-acetyl-D-galactosamine + H type 3-Sp-biotin
UDP + ?
H type 3-Sp-biotin is the preferred substrate
-
-
?
UDP-N-acetyl-D-galactosamine + L-fucosyl-alpha-1,2-beta-galactosyl-O(CH2)7CH3
UDP + alpha-D-galactosaminyl-1,3-[alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
UDP-N-acetyl-D-galactosamine + lacto-N-fucopentaose I
UDP + N-acetyl-alpha-D-galactosaminyl-1,3-[lacto-N-fucopentaose I]
-
i.e. Fucalpha(1-2)Galbeta(1-3)GlcNAcbeta(1-3)Galbeta(1-4)Glc
-
-
?
UDP-N-acetyl-D-glucosamine + L-fucosyl-alpha-1,2-beta-glucosyl-O(CH2)7CH3
UDP + N-acetyl-alpha-D-glucosaminyl-1,3-[alpha-L-fucosyl-1,2]-beta-D-glucosyl-O(CH2)7CH3
UDP-N-acetylgalactosamine + octyl 3-O-methyl-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
UDP + N-acetyl-alpha-D-galactosamine-1,3-[3-O-methyl-alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
-
-
-
-
?
UDP-N-acetylgalactosamine + octyl 4-O-methyl-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
UDP + N-acetyl-alpha-D-galactosaminyl-1,3-[4-O-methyl-alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
-
-
-
-
?
UDP-N-acetylgalactosamine + octyl alpha-L-xylo-hexopyranosyl-(1-2)-beta-D-galactopyranoside
UDP + N-acetyl-alpha-D-galactosaminyl-1,3-[alpha-L-xylo-hexopyranosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
-
-
-
-
?
UDP-N-acetylgalactosamine + octyl beta-D-arabinopyranosyl-(1-2)-beta-D-galactopyranoside
UDP + N-acetyl-alpha-D-galactosaminyl-1,3-[beta-D-arabinopyranosyl-1,2-beta-D-galactosyl-O(CH2)7CH3]
-
-
-
-
?
additional information
?
-
UDP-N-acetyl-D-galactosamine + 2'-fucosyllactose
UDP + N-acetyl-alpha-D-galactosaminyl-2'-fucosyllactose
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + 2'-fucosyllactose
UDP + N-acetyl-alpha-D-galactosaminyl-2'-fucosyllactose
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + 2'-fucosyllactose
UDP + N-acetyl-alpha-D-galactosaminyl-2'-fucosyllactose
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + alpha-L-fucosyl-1-2-D-galactosyl-O-R
UDP + N-acetyl-alpha-D-galactosaminyl-1,3-[alpha-L-fucosyl-1-2]-D-galactosyl-O-R
H-antigen disaccharide
-
-
?
UDP-N-acetyl-D-galactosamine + alpha-L-fucosyl-1-2-D-galactosyl-O-R
UDP + N-acetyl-alpha-D-galactosaminyl-1,3-[alpha-L-fucosyl-1-2]-D-galactosyl-O-R
H-antigen disaccharide, Leu226 is responsible for substrate specificity for UDP-N-acetyl-D-galactosamine as donor substrate, acceptor substrate binding pocket structure, overview
-
-
?
UDP-N-acetyl-D-galactosamine + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein N-acetyl-alpha-D-galactosaminyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein N-acetyl-alpha-D-galactosaminyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
-
-
-
?
UDP-N-acetyl-D-galactosamine + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein N-acetyl-alpha-D-galactosaminyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
-
-
-
?
UDP-N-acetyl-D-galactosamine + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein N-acetyl-alpha-D-galactosaminyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
-
-
-
?
UDP-N-acetyl-D-galactosamine + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein N-acetyl-alpha-D-galactosaminyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
-
-
-
?
UDP-N-acetyl-D-galactosamine + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein N-acetyl-alpha-D-galactosaminyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
-
-
-
?
UDP-N-acetyl-D-galactosamine + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein N-acetyl-alpha-D-galactosaminyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein N-acetyl-alpha-D-galactosaminyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein N-acetyl-alpha-D-galactosaminyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
-
-
-
?
UDP-N-acetyl-D-galactosamine + glycoprotein-alpha-L-fucosyl-(1,2)-D-galactose
UDP + glycoprotein-N-acetyl-alpha-D-galactosaminyl-(1,3)-[alpha-L-fucosyl-(1,2)]-D-galactose
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + glycoprotein-alpha-L-fucosyl-(1,2)-D-galactose
UDP + glycoprotein-N-acetyl-alpha-D-galactosaminyl-(1,3)-[alpha-L-fucosyl-(1,2)]-D-galactose
-
substrate is the histo-blood H group antigen
product is the histo-blood A group antigen
-
?
UDP-N-acetyl-D-galactosamine + glycoprotein-alpha-L-fucosyl-(1,2)-D-galactose
UDP + glycoprotein-N-acetyl-alpha-D-galactosaminyl-(1,3)-[alpha-L-fucosyl-(1,2)]-D-galactose
-
substrate is the histo-blood H group antigen. Arg176 of the enzyme is not important in determining the sugar specificity of enzyme, while Gly235 is influential and Leu266 and Gly268 are crucial in the determination of GalNAc/galactose specificity
product is the histo-blood A group antigen
-
?
UDP-N-acetyl-D-galactosamine + L-fucosyl-alpha-1,2-beta-galactosyl-O(CH2)7CH3
UDP + alpha-D-galactosaminyl-1,3-[alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + L-fucosyl-alpha-1,2-beta-galactosyl-O(CH2)7CH3
UDP + alpha-D-galactosaminyl-1,3-[alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
-
-
-
?
UDP-N-acetyl-D-glucosamine + L-fucosyl-alpha-1,2-beta-glucosyl-O(CH2)7CH3
UDP + N-acetyl-alpha-D-glucosaminyl-1,3-[alpha-L-fucosyl-1,2]-beta-D-glucosyl-O(CH2)7CH3
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + L-fucosyl-alpha-1,2-beta-glucosyl-O(CH2)7CH3
UDP + N-acetyl-alpha-D-glucosaminyl-1,3-[alpha-L-fucosyl-1,2]-beta-D-glucosyl-O(CH2)7CH3
-
-
-
?
additional information
?
-
-
the enzyme possesses flexible substrate specificity
-
-
?
additional information
?
-
-
enzyme also catalyzes the transfer of galactose in alpha-linkage to 2'-fucosyllactose, the transfer rate of galactose is much lower than that of N-acetylgalactosamine
-
-
?
additional information
?
-
-
effective acceptor substrates contain a subterminal beta-galactosyl residue substituted at the O-2 position with fucose
-
-
?
additional information
?
-
-
transfers N-acetylgalactosamine from UDP-N-acetylgalactosamine to H-active structures to form A determinants
-
-
?
additional information
?
-
transfers N-acetylgalactosamine from UDP-N-acetylgalactosamine to H-active structures to form A determinants
-
-
?
additional information
?
-
the enzyme catalyzes the final step in the enzymatic synthesis of the ABO(H) blood group A antigen, overview
-
-
?
additional information
?
-
substrate binding structure by wild-type and mutant GTA, overview
-
-
?
additional information
?
-
-
galactose is used as an acceptor analogue and UDP as a donor analogue in all soaking trials
-
-
?
additional information
?
-
mouse ABO gene-encoded cis-AB transferase contains the GlyGlyAla tripeptide sequence, which is also found in the majority of GBGT1 genes encoding Forssman glycolipid synthase, EC 2.4.1.88. Mouse cis-AB transferase with the GlyGlyAla tripeptide sequence, but not the human cis-AB transferase with the LeuGlyAla, exhibits Forssman glycolipid synthase activity equivalent of mouse GBGT1 gene-encoded Forssman glycolipid synthase
-
-
-
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Breast Neoplasms
A sequencing strategy for the localization of O-glycosylation sites of MUC1 tandem repeats by PSD-MALDI mass spectrometry.
Carcinogenesis
UDP-GalNAc:Fuc alpha 1-2Gal alpha 1-3GalNAc transferase activity in hamster pancreatic cancers and in normal hamster alimentary tissues.
Carcinoma, Hepatocellular
Acetoacetate coenzyme A transferase activity in rat hepatomas.
Carcinoma, Hepatocellular
Regulation of succinyl coenzyme A:acetoacetyl coenzyme A transferase in rat hepatoma cell lines.
Carcinoma, Hepatocellular
Subcellular localization of acetoacetate coenzyme A transferase in rat hepatomas.
Galactosemias
Transferase-deficiency galactosemia: evidence for the lack of a transferase protein in galactosemic red cells.
glycoprotein-fucosylgalactoside alpha-n-acetylgalactosaminyltransferase deficiency
Prenatal diagnosis of succinyl-coenzyme A:3-ketoacid coenzyme A transferase deficiency.
Infections
Two glycosylation alterations of mouse intestinal mucins due to infection caused by the parasite Nippostrongylus brasiliensis.
Leukemia, Myeloid, Acute
Acute leukemia during pregnancy. Association with immune-mediated thrombocytopenia in mother and infant.
Leukemia, Myeloid, Acute
[A transient change in the blood group accompanied by the decreased activity of A transferase in a case of acute myeloid leukemia]
Lung Neoplasms
m6 A transferase METTL3-induced lncRNA ABHD11-AS1 promotes the Warburg effect of non-small-cell lung cancer.
Measles
Expression of ABO or related antigenic carbohydrates on viral envelopes leads to neutralization in the presence of serum containing specific natural antibodies and complement.
Migraine Disorders
Association of genetic loci for migraine susceptibility in the she people of China.
Myocardial Ischemia
Effect of chronic myocardial ischemia on the activity of carnitine palmitylcoenzyme A transferase of isolated canine heart mitochondria.
Neoplasms
3-Oxo acid coenzyme A transferase activity in brain and tumors of the nervous system.
Neoplasms
ABH blood group antigen expression, synthesis, and degradation in human colonic adenocarcinoma cell lines.
Neoplasms
Deletion of A-antigen in a human cancer cell line is associated with reduced promoter activity of CBF/NF-Y binding region, and possibly with enhanced DNA methylation of A transferase promoter.
Neoplasms
Incompatible A antigen expressed in tumors of blood group O individuals: immunochemical, immunohistologic, and enzymatic characterization.
Neoplasms
Loss of acetoacetate coenzyme A transferase activity in tumours of peripheral tissues.
Neoplasms
Targeted breast cancer therapy by harnessing the inherent blood group antigen immune system.
Neoplasms
UDP-GalNAc:Fuc alpha 1-2Gal alpha 1-3GalNAc transferase activity in hamster pancreatic cancers and in normal hamster alimentary tissues.
Nervous System Neoplasms
3-Oxo acid coenzyme A transferase activity in brain and tumors of the nervous system.
Pancreatic Neoplasms
UDP-GalNAc:Fuc alpha 1-2Gal alpha 1-3GalNAc transferase activity in hamster pancreatic cancers and in normal hamster alimentary tissues.
Parasitic Diseases
Blood group A glycosyltransferase occurring as alleles with high sequence difference is transiently induced during a Nippostrongylus brasiliensis parasite infection.
Phenylketonurias
When one disease is not enough: succinyl-CoA: 3-oxoacid coenzyme A transferase (SCOT) deficiency due to a novel mutation in OXCT1 in an infant with known phenylketonuria.
Stomach Neoplasms
Expression of human histo-blood group ABO genes is dependent upon DNA methylation of the promoter region.
Stomach Neoplasms
m6 A transferase KIAA1429-stabilized LINC00958 accelerates gastric cancer aerobic glycolysis through targeting GLUT1.
Stomach Neoplasms
Transcription starting from an alternative promoter leads to the expression of the human ABO histo-blood group antigen.
Tremor
Cryopreservation of spermatozoa from closed colonies, and inbred, spontaneous mutant, and transgenic strains of rats.
Tuberculosis
Potential mechanism of action of meso-dihydroguaiaretic acid on Mycobacterium tuberculosis H37Rv.
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0.27 - 0.47
2'-fucosyllactose
0.0099 - 0.4
alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
1.3
alpha-L-Fucp-(1,2)-beta-D-Galp-(1,3)-beta-DGlcNAcp-O(CH2)7CH3
37°C, pH 7.0
0.49
alpha-L-Fucp-(1,2)-beta-D-Galp-(1,4)-beta-D-GlcNAcp-O-(CH2)8CO2CH3
37°C, pH 7.0
0.087
alpha-L-Fucp-(1,2)-beta-D-Galp-O(CH2)7CH3
37°C, pH 7.0
0.0087 - 0.167
L-fucosyl-alpha-1,2-beta-galactosyl-O(CH2)7CH3
0.35
lacto-N-fucopentaose I
-
-
0.02
octyl 3-O-methyl-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
-
-
1.14
octyl 4-O-methyl-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
-
-
0.208
octyl beta-D-arabinopyranosyl-(1-2)-beta-D-galactopyranoside
-
-
0.0087 - 0.086
UDP-N-acetyl-alpha-D-galactosamine
additional information
additional information
kinetics of recombinant wild-type GTA 53-354 and of GTA/GTB mutant chimeric enzymes
-
0.27
2'-fucosyllactose
-
-
0.39
2'-fucosyllactose
-
distal colon
0.47
2'-fucosyllactose
-
pancreatic cancer cell line
0.0099
alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
wild-type, pH 7.0, 37°C
0.036
alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
mutant E303Q, pH 7.0, 37°C
0.045
alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
mutant D302C, pH 7.0, 37°C
0.099
alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
wild-type, pH 7.0, 37°C
0.27
alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
mutant E303D, pH 7.0, 37°C
0.4
alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
mutant E303C, pH 7.0, 37°C
0.0087
L-fucosyl-alpha-1,2-beta-galactosyl-O(CH2)7CH3
-
0.013
L-fucosyl-alpha-1,2-beta-galactosyl-O(CH2)7CH3
-
-
0.144
L-fucosyl-alpha-1,2-beta-galactosyl-O(CH2)7CH3
-
0.167
L-fucosyl-alpha-1,2-beta-galactosyl-O(CH2)7CH3
G176R/P234S/S235G/M266L/A268G mutant
0.0099
UDP-GalNAc
-
0.048
UDP-GalNAc
-
pancreatic cancer cell line, distal colon
3.74
UDP-GalNAc
G176R/P234S/S235G/M266L/A268G mutant
0.0087
UDP-N-acetyl-alpha-D-galactosamine
wild-type, pH 7.0, 37°C
0.0087
UDP-N-acetyl-alpha-D-galactosamine
wild-type, pH 7.0, 37°C
0.022
UDP-N-acetyl-alpha-D-galactosamine
mutant D302C, pH 7.0, 37°C
0.03
UDP-N-acetyl-alpha-D-galactosamine
mutant E303A, pH 7.0, 37°C
0.05
UDP-N-acetyl-alpha-D-galactosamine
mutant E303Q, pH 7.0, 37°C
0.051
UDP-N-acetyl-alpha-D-galactosamine
mutant E303C, pH 7.0, 37°C
0.086
UDP-N-acetyl-alpha-D-galactosamine
mutant E303D, pH 7.0, 37°C
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a large single crystal is subjected to H/D exchange prior to data collection and time-of-flight neutron diffraction data is collected to 2.5 A resolution at the Protein Crystallography Station to 85% overall completeness, with complementary X-ray diffraction data collected from a crystal from the same drop and extending to 1.85 A resolution
assignment of all methyl resonance signals in Ala, Ile, Leu, Met and Val labeled samples of GTA and GTB by lanthanide-induced pseudocontact shifts and methyl-methyl NOESY. The fully closed state is not adopted in the presence of lanthanide ions
crystals of purified native enzyme are soaked with various combinations of UDP-GalNAc, UDP-Gal, UDP, and acceptor analogues alpha-L-fucosyl-1-2-beta-D-(3-deoxy)-galactosyl-O-R or alpha-L-fucosyl-1-2-beta-D-(3-amino)-galactosyl-O-R, ligands are solved in 7.5% PEG 4000, 15% glycerol, 75 mM N-[2-acetamido]-2-iminodiacetic acid, pH 7.5, 10 mM MnCl2, and 10 mM inhibitor, 3-4 days, X-ray diffraction structure determination and analysis at 2.1 A resolution
enzyme adopts an open conformation in the absence of substrates. Binding of UDP induces a semiclosed conformation. In the presence of both donor and acceptor substrates, the enzymes shift towards a closed conformation with ordering of an internal loop and the C-terminal residues, which then completely cover the donor-binding pocket. The enzyme shows substantial plasticity and conformational flexibility. Residues Ile123 at the bottom of the UDP binding pocket, and Ile192 as part of the internal loop are significantly disturbed upon stepwise addition of UDP and H-disaccharide-O-CH3
enzyme soaked with acceptor analogs: galactose, lactose, N-acetyllactosamine, beta-D-Galp-O(CH2)8CO2CH3, alpha-L-Fucp-(1,2)-beta-D-Galp-O(CH2)7CH3, beta-D-Galp-(1,4)-beta-D-Glcp-OCH3, alpha-L-Fucp-(1,2)-beta-D-Galp-(1,3)-beta-D-GlcNAcp-O(CH2)7CH3, alpha-L-Fucp-(1,2)-beta-D-Galp-(1,4)-beta-D-GlcNAcp-O-(CH2)8CO2CH3
G176R/P234S/S235G/M266L/A268G-mutant with and without H-antigen, at 1.55 and 1.65 A resolution respectively
Methyl-TROSY-based titration experiments in combination with zz-exchange experiments show dramatic changes of binding kinetics associated with allosteric interactions between donor-type and acceptor-type ligands. Binding of the acceptor substrates H-disaccharide, H-type II trisaccharide, and H-type VI trisaccharide affects the chemical shifts of the 13C-methyl groups of Met 266, Val 299, Leu 324, and Leu 329, which belong to the acceptor substrate binding pocket. Depending on substrate concentrations in the Golgi apparatus an acceptor route and a donor route are possible. At high local concentrations of UDP-Gal or UDP-GalNAc binding of the nucleotide sugar to GTB or GTA would precede binding of the H-antigen. At low nucleotide sugar concentrations, it can be assumed that H-antigen binds first. In this latter case, the enzymes may discriminate between different types of H-antigens, preferring e. g. type-II over type-I H-antigens
of catalytic domain residues 63-354, with and without L-fucosyl-alpha-1,2-beta-galactosyl-O(CH2)7CH3-acceptor and UDP, at 1.35 and 1.8 A resolution respectively
purified recombinant GTA/GTB mutant chimeric enzymes, complexing with synthetic antigen disaccharides or UDP, hanging drop vapour diffusion method, different solutions for the different chimeric mutants, X-ray diffraction structure determinationand analysis at 1.41-1.75 A resolution, overview, structure modelling
structures of GTA, GTB and several chimeras determined by single-crystal X-ray diffraction demonstrate a range of susceptibility to the choice of cryoprotectant, in which the mobile polypeptide loops can be induced by glycerol to form the ordered closed conformation associated with substrate recognition and by MPD (hexylene glycol, 2-methyl-2,4-pentanediol) to hinder binding of substrate in the active site owing to chelation of the Mn2+ cofactor and thereby adopt the disordered open state
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structures of isoforms GTA and GTB in complex with their respective trisaccharide products. A conflict exists between the transferred sugar monosaccharide and the beta-phosphate of the UDP donor. The mechanism of product release shows monosaccharide transfer to the H-antigen acceptor induces active site disorder and ejection of the UDP leaving group prior to trisaccharide egress
structures of wild-type and mutant D302C. Conserved active site residues Arg188 and Asp302 are critical for catalysis, and disruption of their hydrogen bond network through mutation can dramatically decrease enzymatic activity
wild-type and mutants E303A, E303C, E303D, E303Q
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D302A
almost complete loss of activity
D302A/D316A
very low residual activity
D302C
kcat value is 9.5% that of wild-type GTB
D302E
kcat value is 47% that of wild-type GTB
D302E/D316E
almost complete loss of activity
D302L
almost complete loss of activity
D302N
almost complete loss of activity
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
G176R/P234S/S235G/M266L/A268G
expressed in Escherichia coli BL21, although 4 of the mutations correspond to a change from A- to B-blood group, the P234S-mutation shows a remarkable increase in A-donor specificity
R188K
almost complete loss of activity
additional information
construction of GTA/GTB chimeric enzymes GTB/G176R and GTB/G176R/G235S
additional information
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generation of a chimeric histo-blood group B transferase by replacing the N-acetyl-D-galactosamine recognition domain of human A transferase with the galactose-recognition domain of evolutionarily related murine alpha1,3-galactosyltransferase, the chimeric mutant shows a functional conversion from A to B transferase activity, overview. The AT-MluI-GT construct, which expresses the chimera between the long N-terminal sequence up to the MluI site of human A transferase, and the short C-terminal sequence up to the MluI site of murine a1-3Gal transferase, produces the antigens that react with both the anti-A and the Griffonia simplicifolia Lectin I, GSL-IA4, lectin
additional information
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chimeric GTA and GTB enzymes are generated (AABB, ABBA and ABBB)
additional information
amino acids at codons 266 and 268 of human isoforms GTA, EC 2.4.1.40, and GTB, EC 2.4.1.37, are crucial to their distinct sugar specificities. In vitro mutagenized GTAs/GTBs having any of 20 possible amino acids at those codons show that those codons determine the transferase activity and sugar specificity
additional information
expression of constructs, having either of AlaGlyGly, GlyGlyAla, HisAlaAla, LeuGlyGly, or MetGlyAla tripeptide sequence at codons corresponding to 266-268 of human GTA/GTB. The original human GTA construct with LeuGlyGly and the substitution construct with AlaGlyGly exhibit strong GTA. Human GTA constructs with GlyGlyAla, HisAlaAla, LeuGlyGly, or MetGlyAla exhibit GTA, GTA/GTB, GTB, GTA, or GTB activity, respectively
additional information
preparation of human GTA derivative constructs containing any of the 20 amino acids at codon 69 with and without a GlyGlyAla substitution of the LeuGlyGly tripeptide at codons 266-268. In presence of the Forssman glycolipid synthase substrate, all substitution constructs at codon 69 exhibit Forssman glycolipid synthase activity. The combination with tripeptide GlyGlyAla substitution significantly increases the activity. With increased globoside availability, the native human GTA with a methionine residue at codon 69 also synthesizes Forssman antigen
additional information
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preparation of human GTA derivative constructs containing any of the 20 amino acids at codon 69 with and without a GlyGlyAla substitution of the LeuGlyGly tripeptide at codons 266-268. In presence of the Forssman glycolipid synthase substrate, all substitution constructs at codon 69 exhibit Forssman glycolipid synthase activity. The combination with tripeptide GlyGlyAla substitution significantly increases the activity. With increased globoside availability, the native human GTA with a methionine residue at codon 69 also synthesizes Forssman antigen
additional information
the enzymes GTA, EC 2.4.1.40, and GTB have nearly identical sequences, while the corresponding mutants of GTA/GTB have up to a 13fold difference in their residual activities relative to wild type.The mutated Cys, Asp and Gln functional groups are no more than 0.8 A further from the anomeric carbon of donor substrate compared to wild type
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