The Enzyme Database

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EC 2.8.2.35     
Accepted name: dermatan 4-sulfotransferase
Reaction: 3′-phospho-5′-adenylyl sulfate + [dermatan]-N-acetyl-D-galactosamine = adenosine 3′,5′-bisphosphate + [dermatan]-4-O-sulfo-N-acetyl-D-galactosamine
Other name(s): dermatan-specific N-acetylgalactosamine 4-O-sulfotransferase; dermatan-4-sulfotransferase-1; dermatan-4-sulfotransferase 1; D4ST-1; dermatan N-acetylgalactosamine 4-O-sulfotransferase; CHST14 protein; CHST14
Systematic name: 3′-phospho-5′-adenylyl sulfate:[dermatan]-N-acetyl-D-galactosamine 4-sulfotransferase
Comments: The sulfation takes place at the 4-position of N-acetyl-D-galactosamine residues of dermatan. D4ST-1 shows a strong preference in vitro for sulfate transfer to IdoUAα(1,3)GalNAcβ(1,4) that is flanked by GlcUAβ(1,3)GalNAcβ(1,4) as compared with IdoUAα(1,3)GalNAcβ(1,4) flanked by IdoUAα(1,3)GalNAcβ(1,4) [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Evers, M.R., Xia, G., Kang, H.G., Schachner, M. and Baenziger, J.U. Molecular cloning and characterization of a dermatan-specific N-acetylgalactosamine 4-O-sulfotransferase. J. Biol. Chem. 276 (2001) 36344–36353. [PMID: 11470797]
2.  Mikami, T., Mizumoto, S., Kago, N., Kitagawa, H. and Sugahara, K. Specificities of three distinct human chondroitin/dermatan N-acetylgalactosamine 4-O-sulfotransferases demonstrated using partially desulfated dermatan sulfate as an acceptor: implication of differential roles in dermatan sulfate biosynthesis. J. Biol. Chem. 278 (2003) 36115–36127. [PMID: 12847091]
3.  Pacheco, B., Maccarana, M. and Malmstrom, A. Dermatan 4-O-sulfotransferase 1 is pivotal in the formation of iduronic acid blocks in dermatan sulfate. Glycobiology 19 (2009) 1197–1203. [PMID: 19661164]
4.  Mitsunaga, C., Mikami, T., Mizumoto, S., Fukuda, J. and Sugahara, K. Chondroitin sulfate/dermatan sulfate hybrid chains in the development of cerebellum. Spatiotemporal regulation of the expression of critical disulfated disaccharides by specific sulfotransferases. J. Biol. Chem. 281 (2006) 18942–18952. [PMID: 16702220]
[EC 2.8.2.35 created 2010]
 
 


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