Beta-1,3-galactosyltransferase 4 is an
enzyme that in humans is encoded by the B3GALT4gene.[5][6]
This gene is a member of the beta-1,3-
galactosyltransferase (beta3GalT) gene family. This family encodes type II
membrane-boundglycoproteins with diverse enzymatic functions using different donor substrates (
UDP-galactose and
UDP-N-acetylglucosamine) and different acceptor sugars (
N-acetylglucosamine,
galactose,
N-acetylgalactosamine). The beta3GalT genes are distantly related to the Drosophila Brainiac gene and have the protein
coding sequence contained in a single
exon. The beta3GalT proteins also contain
conserved sequences not found in the beta4GalT or alpha3GalT proteins. The carbohydrate chains synthesized by these enzymes are designated as type 1, whereas beta4GalT enzymes synthesize type 2 carbohydrate chains. The ratio of type 1:type 2 chains changes during
embryogenesis. By
sequence similarity, the beta3GalT genes fall into at least two groups: beta3GalT4 and 4 other beta3GalT genes (beta3GalT1-3, beta3GalT5). This gene is oriented
telomere to
centromere in close proximity to the
ribosomal protein S18 gene. The functionality of the encoded protein is limited to ganglioseries
glycolipidbiosynthesis.[6]
Amado M, Almeida R, Schwientek T, Clausen H (2000). "Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions". Biochim. Biophys. Acta. 1473 (1): 35–53.
doi:
10.1016/S0304-4165(99)00168-3.
PMID10580128.
Shiina T, Kikkawa E, Iwasaki H, et al. (2000). "The beta-1,3-galactosyltransferase-4 (B3GALT4) gene is located in the centromeric segment of the human MHC class II region". Immunogenetics. 51 (1): 75–8.
doi:
10.1007/s002510050012.
PMID10663566.
S2CID35331402.
Robinson WE, Montefiori DC, Mitchell WM (1988). "Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis". AIDS Res. Hum. Retroviruses. 3 (3): 265–82.
doi:
10.1089/aid.1987.3.265.
PMID2829950.
Kozarsky K, Penman M, Basiripour L, et al. (1989). "Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein". J. Acquir. Immune Defic. Syndr. 2 (2): 163–9.
PMID2649653.
Beta-1,3-galactosyltransferase 4 is an
enzyme that in humans is encoded by the B3GALT4gene.[5][6]
This gene is a member of the beta-1,3-
galactosyltransferase (beta3GalT) gene family. This family encodes type II
membrane-boundglycoproteins with diverse enzymatic functions using different donor substrates (
UDP-galactose and
UDP-N-acetylglucosamine) and different acceptor sugars (
N-acetylglucosamine,
galactose,
N-acetylgalactosamine). The beta3GalT genes are distantly related to the Drosophila Brainiac gene and have the protein
coding sequence contained in a single
exon. The beta3GalT proteins also contain
conserved sequences not found in the beta4GalT or alpha3GalT proteins. The carbohydrate chains synthesized by these enzymes are designated as type 1, whereas beta4GalT enzymes synthesize type 2 carbohydrate chains. The ratio of type 1:type 2 chains changes during
embryogenesis. By
sequence similarity, the beta3GalT genes fall into at least two groups: beta3GalT4 and 4 other beta3GalT genes (beta3GalT1-3, beta3GalT5). This gene is oriented
telomere to
centromere in close proximity to the
ribosomal protein S18 gene. The functionality of the encoded protein is limited to ganglioseries
glycolipidbiosynthesis.[6]
Amado M, Almeida R, Schwientek T, Clausen H (2000). "Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions". Biochim. Biophys. Acta. 1473 (1): 35–53.
doi:
10.1016/S0304-4165(99)00168-3.
PMID10580128.
Shiina T, Kikkawa E, Iwasaki H, et al. (2000). "The beta-1,3-galactosyltransferase-4 (B3GALT4) gene is located in the centromeric segment of the human MHC class II region". Immunogenetics. 51 (1): 75–8.
doi:
10.1007/s002510050012.
PMID10663566.
S2CID35331402.
Robinson WE, Montefiori DC, Mitchell WM (1988). "Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis". AIDS Res. Hum. Retroviruses. 3 (3): 265–82.
doi:
10.1089/aid.1987.3.265.
PMID2829950.
Kozarsky K, Penman M, Basiripour L, et al. (1989). "Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein". J. Acquir. Immune Defic. Syndr. 2 (2): 163–9.
PMID2649653.