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Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase








Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase


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glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase
Identifiers
EC number
2.4.1.122
CAS number
97089-61-7
Databases
IntEnz
IntEnz view
BRENDA
BRENDA entry
ExPASy
NiceZyme view
KEGG
KEGG entry
MetaCyc
metabolic pathway
PRIAM
profile

PDB structures
RCSB PDB PDBe PDBsum
Gene Ontology
AmiGO / QuickGO

















In enzymology, a glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase (EC 2.4.1.122) is an enzyme that catalyzes the chemical reaction


UDP-galactose + glycoprotein N-acetyl-D-galactosamine ⇌{displaystyle rightleftharpoons }rightleftharpoons UDP + glycoprotein D-galactosyl-1,3-N-acetyl-D-galactosamine

Thus, the two substrates of this enzyme are UDP-galactose and glycoprotein N-acetyl-D-galactosamine, whereas its two products are UDP and glycoprotein D-galactosyl-1,3-N-acetyl-D-galactosamine.


This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-galactose:glycoprotein-N-acetyl-D-galactosamine 3-beta-D-galactosyltransferase. This enzyme is also called uridine diphosphogalactose-mucin beta-(1->3)-galactosyltransferase. This enzyme participates in o-glycan biosynthesis and glycan structures - biosynthesis 1.



See also[edit]


  • C1GALT1


References[edit]






  • Hesford FJ, Berger EG, Van den Eijnden DH (1981). "Identification of the product formed by human erythrocyte galactosyltransferase". Biochim. Biophys. Acta. 659 (2): 302&ndash, 11. doi:10.1016/0005-2744(81)90056-5. PMID 6789880..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output q{quotes:"""""""'""'"}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-limited a,.mw-parser-output .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{font-size:100%}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}


  • Mendicino J, Sivakami S, Davila M, Chandrasekaran EV (1982). "Purification and properties of UDP-gal:N-acetylgalactosaminide mucin: beta 1,3-galactosyltransferase from swine trachea mucosa". J. Biol. Chem. 257 (7): 3987&ndash, 94. PMID 6801057.


  • Schachter H, Narasimhan S, Gleeson P, Vella G (1983). "Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type". Methods Enzymol. 98: 98&ndash, 134. doi:10.1016/0076-6879(83)98143-0. PMID 6366476.












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