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Information on EC 2.4.1.79 - globotriaosylceramide 3-beta-N-acetylgalactosaminyltransferase and Organism(s) Homo sapiens and UniProt Accession O75752

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IUBMB Comments
Globoside is a neutral glycosphingolipid in human erythrocytes and has blood-group-P-antigen activity . The enzyme requires a divalent cation for activity, with Mn2+ required for maximal activity . UDP-GalNAc is the only sugar donor that is used efficiently by the enzyme: UDP-Gal and UDP-GlcNAc result in very low enzyme activity . Lactosylceramide, globoside and gangliosides GM3 and GD3 are not substrates . For explanation of the superscripted '3' in the systematic name, see {iupac/misc/glylp#5.3::GL-5.3.4}.
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Homo sapiens
UNIPROT: O75752
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
globoside synthetase, udp-n-acetylgalactosamine:globotriaosylceramide beta-3-n-acetylgalactosaminyltransferase, udp-n-acetylgalactosamine:globotriaosylceramide 3-beta-n-acetylgalactosaminyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylgalactosaminyltransferase, uridine diphosphoacetylgalactosamine-galactosylgalactosylglucosylceramide
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acetylgalactosaminyltransferase, uridine diphosphoacetylgalactosamine-glycosphingolipid
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galactosylgalactosylglucosylceramide beta-D-acetylgalactosaminyltransferase
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GalNAc transferase
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globoside N-acetylgalactosaminyltransferase
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globoside synthetase
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glycosphingolipid beta-N-acetylgalactosaminyltransferase
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UDP-N-acetylgalactosamine:globotriaosylceramide 3-beta-N-acetylgalactosaminyltransferase
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UDP-N-acetylgalactosamine:globotriaosylceramide beta-3-N-acetylgalactosaminyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-galactosamine:alpha-D-galactosyl-(1->4)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide III3-beta-N-acetyl-D-galactosaminyltransferase
Globoside is a neutral glycosphingolipid in human erythrocytes and has blood-group-P-antigen activity [4]. The enzyme requires a divalent cation for activity, with Mn2+ required for maximal activity [3]. UDP-GalNAc is the only sugar donor that is used efficiently by the enzyme: UDP-Gal and UDP-GlcNAc result in very low enzyme activity [3]. Lactosylceramide, globoside and gangliosides GM3 and GD3 are not substrates [4]. For explanation of the superscripted '3' in the systematic name, see {iupac/misc/glylp#5.3::GL-5.3.4}.
CAS REGISTRY NUMBER
COMMENTARY hide
62213-46-1
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83215-90-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-galactosamine + D-galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide
UDP + N-acetyl-D-galactosaminyl-1,3-D-galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-galactosamine + D-galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide
UDP + N-acetyl-D-galactosaminyl-1,3-D-galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide
show the reaction diagram
the enzyme is responsible for synthesis of P blood group antigen. Mutations capable of abolishing enzyme function are present in individuals with the Pk phenotype
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
B3GL1_HUMAN
331
1
39512
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39511
x * 39511, calculation from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 39511, calculation from nucleotide sequence
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the enzyme contains five potential N-linked glycosylation sites
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hellberg, A.; Poole, J.; Olsson, M.L.
Molecular basis of the globoside-deficient Pk blood group phenotype: Identification of four inactivating mutations in the UDP-N-acetylgalactosamine:globotriaosylceramide 3-beta-N-acetylgalactosaminyltransferase gene
J. Biol. Chem.
277
29455-29459
2002
Homo sapiens (O75752)
Manually annotated by BRENDA team
Okajima, T.; Nakamura, Y.; Uchikawa, M.; Haslam, D.B.; Numata, S.I.; Furukawa, K.; Urano, T.; Furukawa, K.
Expression cloning of human globoside synthase cDNAs. Identification of beta 3Gal-T3 as UDP-N-acetylgalactosamine:globotriaosylceramide beta 1,3-N-acetylgalactosaminyltransferase
J. Biol. Chem.
275
40498-40503
2000
Homo sapiens (O75752)
Manually annotated by BRENDA team