[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/b4galt1-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/b4galt1-wikipedia\/","headline":"B4GALT1 – Wikipedia","name":"B4GALT1 – Wikipedia","description":"before-content-x4 From Wikipedia, the free encyclopedia after-content-x4 Protein-coding gene in the species Homo sapiens B4GALT1 Available structures PDB Ortholog search:","datePublished":"2021-01-02","dateModified":"2021-01-02","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/thumb\/d\/d1\/Protein_B4GALT1_PDB_1nf5.png\/250px-Protein_B4GALT1_PDB_1nf5.png","url":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/thumb\/d\/d1\/Protein_B4GALT1_PDB_1nf5.png\/250px-Protein_B4GALT1_PDB_1nf5.png","height":"145","width":"250"},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/b4galt1-wikipedia\/","about":["Wiki"],"wordCount":7985,"articleBody":"     (adsbygoogle = window.adsbygoogle || []).push({});before-content-x4From Wikipedia, the free encyclopedia       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Protein-coding gene in the species Homo sapiensB4GALT1Available structuresPDBOrtholog search: PDBe RCSB List of PDB id codes2AE7, 2AEC, 2AES, 2AGD, 2AH9, 2FY7, 2FYA, 2FYB, 3EE5, 4EE3, 4EE4, 4EE5, 4EEA, 4EEG, 4EEM, 4EEO, 4L41       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4IdentifiersAliasesB4GALT1, B4GAL-T1, CDG2D, GGTB2, GT1, GTB, beta4Gal-T1, beta-1,4-galactosyltransferase 1External IDsOMIM: 137060 MGI: 95705 HomoloGene: 20378 GeneCards: B4GALT1 RNA expression patternBgeeHumanMouse (ortholog)Top expressed instromal cell of endometriumleft uterine tubeminor salivary glandgallbladder       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4smooth muscle tissueleft lobe of thyroid glandright lobe of thyroid glandright lobe of liverupper lobe of left lungright lungTop expressed inlacrimal glandpyloric antrummucous cell of stomachcumulus cellcrypt of lieberkuhn of small intestinesubmandibular glandintestinal villusmolarconjunctival fornixplacentaMore reference expression dataBioGPSWikidataBeta-1,4-galactosyltransferase 1 is an enzyme that in humans is encoded by the B4GALT1 gene.[5][6]This gene is one of seven beta-1,4-galactosyltransferase (beta4GalT) genes. They encode type II membrane-bound glycoproteins that appear to have exclusive specificity for the donor substrate UDP-galactose; all transfer galactose in a beta1,4 linkage to similar acceptor sugars: GlcNAc, Glc, and Xyl. Each beta4GalT has a distinct function in the biosynthesis of different glycoconjugates and saccharide structures. As type II membrane proteins, they have an N-terminal hydrophobic signal sequence that directs the protein to the Golgi apparatus and which then remains uncleaved to function as a transmembrane anchor. By sequence similarity, the beta4GalTs form four groups: beta4GalT1 and beta4GalT2, beta4GalT3 and beta4GalT4, beta4GalT5 and beta4GalT6, and beta4GalT7. This gene is unique among the beta4GalT genes because it encodes an enzyme that participates both in glycoconjugate and lactose biosynthesis. For the first activity, the enzyme adds galactose to N-acetylglucosamine residues that are either monosaccharides or the nonreducing ends of glycoprotein carbohydrate chains. The second activity is restricted to lactating mammary tissues where the enzyme forms a heterodimer with alpha-lactalbumin to catalyze UDP-galactose + D-glucose  UDP + lactose. The two enzymatic forms result from alternate transcription initiation sites and post-translational processing. Two transcripts, which differ only at the 5′ end, with approximate lengths of 4.1 kb and 3.9 kb encode the same protein. The longer transcript encodes the type II membrane-bound, trans-Golgi resident protein involved in glycoconjugate biosynthesis. The shorter transcript encodes a protein which is cleaved to form the soluble lactose synthase.[6]References[edit]Further reading[edit]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\u201353. doi:10.1016\/S0304-4165(99)00168-3. PMID\u00a010580128.Gerber AC, Kozdrowski I, Wyss SR, Berger EG (1979). “The charge heterogeneity of soluble human galactosyltransferases isolated from milk, amniotic fluid and malignant ascites”. Eur. J. Biochem. 93 (3): 453\u201360. doi:10.1111\/j.1432-1033.1979.tb12843.x. PMID\u00a033805.Uejima T, Uemura M, Nozawa S, Narimatsu H (1992). “Complementary DNA cloning for galactosyltransferase associated with tumor and determination of antigenic epitopes recognized by specific monoclonal antibodies”. Cancer Res. 52 (22): 6158\u201363. PMID\u00a01384956.Lopez LC, Youakim A, Evans SC, Shur BD (1991). “Evidence for a molecular distinction between Golgi and cell surface forms of beta 1,4-galactosyltransferase”. J. Biol. Chem. 266 (24): 15984\u201391. doi:10.1016\/S0021-9258(18)98505-4. PMID\u00a01714903.Mengle-Gaw L, McCoy-Haman MF, Tiemeier DC (1991). “Genomic structure and expression of human beta-1,4-galactosyltransferase”. Biochem. Biophys. Res. Commun. 176 (3): 1269\u201376. doi:10.1016\/0006-291X(91)90423-5. PMID\u00a01903938.Aoki D, Appert HE, Johnson D,  et\u00a0al. (1990). “Analysis of the substrate binding sites of human galactosyltransferase by protein engineering”. EMBO J. 9 (10): 3171\u20138. doi:10.1002\/j.1460-2075.1990.tb07515.x. PMC\u00a0552046. PMID\u00a02120039.Watzele G, Berger EG (1991). “Near identity of HeLa cell galactosyltransferase with the human placental enzyme”. Nucleic Acids Res. 18 (23): 7174. doi:10.1093\/nar\/18.23.7174. PMC\u00a0332820. PMID\u00a02124683.Kalyanaraman VS, Rodriguez V, Veronese F,  et\u00a0al. (1990). “Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1”. AIDS Res. Hum. Retroviruses. 6 (3): 371\u201380. doi:10.1089\/aid.1990.6.371. PMID\u00a02187500.Pal R, Hoke GM, Sarngadharan MG (1989). “Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1”. Proc. Natl. Acad. Sci. U.S.A. 86 (9): 3384\u20138. Bibcode:1989PNAS…86.3384P. doi:10.1073\/pnas.86.9.3384. PMC\u00a0287137. PMID\u00a02541446.Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP (1989). “Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport”. J. Virol. 63 (6): 2452\u20136. doi:10.1128\/jvi.63.6.2452-2456.1989. PMC\u00a0250699. PMID\u00a02542563.Kozarsky K, Penman M, Basiripour L,  et\u00a0al. (1989). “Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein”. J. Acquir. Immune Defic. Syndr. 2 (2): 163\u20139. PMID\u00a02649653.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\u201382. doi:10.1089\/aid.1987.3.265. PMID\u00a02829950.Appert HE, Rutherford TJ, Tarr GE,  et\u00a0al. (1986). “Isolation of galactosyltransferase from human milk and the determination of its N-terminal amino acid sequence” (PDF). Biochem. Biophys. Res. Commun. 138 (1): 224\u20139. doi:10.1016\/0006-291X(86)90269-X. hdl:2027.42\/26099. PMID\u00a03091013.Appert HE, Rutherford TJ, Tarr GE,  et\u00a0al. (1986). “Isolation of a cDNA coding for human galactosyltransferase” (PDF). Biochem. Biophys. Res. Commun. 139 (1): 163\u20138. doi:10.1016\/S0006-291X(86)80094-8. hdl:2027.42\/26068. PMID\u00a03094506.Furukawa K, Roth S, Sawicki J (1987). “Several Galactosyltransferase Activities Are Associated with Mouse Chromosome 17”. Genetics. 114 (3): 983\u201391. doi:10.1093\/genetics\/114.3.983. PMC\u00a01203025. PMID\u00a03098628.Masri KA, Appert HE, Fukuda MN (1989). “Identification of the full-length coding sequence for human galactosyltransferase (beta-N-acetylglucosaminide: beta 1,4-galactosyltransferase)”. Biochem. Biophys. Res. Commun. 157 (2): 657\u201363. doi:10.1016\/S0006-291X(88)80300-0. PMID\u00a03144273.Roth J, Lentze MJ, Berger EG (1985). “Immunocytochemical demonstration of ecto-galactosyltransferase in absorptive intestinal cells”. J. Cell Biol. 100 (1): 118\u201325. doi:10.1083\/jcb.100.1.118. PMC\u00a02113462. PMID\u00a03917437.Roth J, Berger EG (1982). “Immunocytochemical localization of galactosyltransferase in HeLa cells: codistribution with thiamine pyrophosphatase in trans-Golgi cisternae”. J. Cell Biol. 93 (1): 223\u20139. doi:10.1083\/jcb.93.1.223. PMC\u00a02112114. PMID\u00a06121819.Chatterjee SK, Mukerjee S, Tripathi PK (1995). “Analysis of the sequences of human beta-1,4-galactosyltransferase cDNA clones”. Int. J. Biochem. Cell Biol. 27 (3): 329\u201336. doi:10.1016\/1357-2725(94)00062-G. PMID\u00a07540104.Kudo T, Narimatsu H (1995). “The beta 1,4-galactosyltransferase gene is post-transcriptionally regulated during differentiation of mouse F9 teratocarcinoma cells”. Glycobiology. 5 (4): 397\u2013403. doi:10.1093\/glycob\/5.4.397. PMID\u00a07579794.External links[edit]PDB gallery1nf5: Crystal Structure of Lactose Synthase, Complex with Glucose1nhe: Crystal structure of Lactose synthase complex with UDP1nkh: Crystal structure of Lactose synthase complex with UDP and Manganese1nmm: beta-1,4-galactosyltransferase mutant Cys342Thr complex with alpha-lactalbumin and GlcNAc1nqi: crystal structure of lactose synthase, a 1:1 complex between beta1,4-galactosyltransferase and alpha-lactalbumin in the presence of GlcNAc1nwg: BETA-1,4-GALACTOSYLTRANSFERASE COMPLEX WITH ALPHA-LACTALBUMIN AND N-BUTANOYL-GLUCOAMINE1o0r: Crystal structure of the catalytic domain of bovine beta1,4-galactosyltransferase complex with UDP-galactose1o23: CRYSTAL STRUCTURE OF LACTOSE SYNTHASE IN THE PRESENCE OF UDP-GLUCOSE1oqm: A 1:1 complex between alpha-lactalbumin and beta1,4-galactosyltransferase in the presence of UDP-N-acetyl-galactosamine2ae7: Crystal Structure of Human M340H-Beta1,4-Galactosyltransferase-I (M340H-B4GAL-T1) in Complex with Pentasaccharide2aec: Crystal Structure of Human M340H-Beta1,4-Galactosyltransferase-I (M340H-B4GAL-T1) in Complex with GlcNAc-beta1,2-Man-alpha1,6-Man-beta-OR2aes: Crystal Structure of Human M340H-Beta1,4-Galactosyltransferase-I (M340H-B4Gal-T1) in Complex with GlcNAc-beta1,2-Man-alpha1,3-Man-beta-OR2agd: Crystal Structure of Human M340H-Beta-1,4-Galactosyltransferase-I(M340H-B4Gal-T1) in Complex with GlcNAc-beta1,4-Man-alpha1,3-Man-beta-OR2ah9: Crystal Structure of Human M340H-Beta-1,4-Galactosyltransferase-I (M340H-B4Gal-T1) in Complex with Chitotriose2fy7: Crystal structure of the catalytic domain of the human beta1,4-galactosyltransferase mutant M339H in apo form2fya: Crystal structure of the catalytic domain of the human beta1, 4-galactosyltransferase mutant M339H complex with manganese2fyb: Crystal structure of the catalytic domain of the human beta1,4-galactosyltransferase mutant M339H in complex with Mn and UDP-galactose in open conformation       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4"},{"@context":"http:\/\/schema.org\/","@type":"BreadcrumbList","itemListElement":[{"@type":"ListItem","position":1,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/#breadcrumbitem","name":"Enzyklop\u00e4die"}},{"@type":"ListItem","position":2,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/b4galt1-wikipedia\/#breadcrumbitem","name":"B4GALT1 – Wikipedia"}}]}]