Summary: Sulfotransferase family
This is the Wikipedia entry entitled "Carbohydrate sulfotransferase". More...
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Carbohydrate sulfotransferase Edit Wikipedia article
Example carbohydrate sulfotransferase with PAPS cosubstrate and carbohydrate substrate: Crystal Structure of human 3-O-Sulfotransferase-3 with bound PAPS and tetrasaccharide substrate. Enzyme chain A (blue), Enzyme chain B (green), PAPS (red), tetrasaccharide substrate (white), sodium ion (purple sphere).
Carbohydrate sulfotransferases are sulfotransferase enzymes that transfer sulfate to carbohydrate groups in glycoproteins and glycolipids. Carbohydrates are used by cells for a wide range of functions from structural purposes to extracellular communication. Carbohydrates are suitable for such a wide variety of functions due to the diversity in structure generated from monosaccharide composition, glycosidic linkage positions, chain branching, and covalent modification. Possible covalent modifications include acetylation, methylation, phosphorylation, and sulfation. Sulfation, performed by carbohydrate sulfotransferases, generates carbohydrate sulfate esters. These sulfate esters are only located extracellularly, whether through excretion into the extracellular matrix (ECM) or by presentation on the cell surface. As extracellular compounds, sulfated carbohydrates are mediators of intercellular communication, cellular adhesion, and ECM maintenance.
Sulfotransferases catalyze the transfer of a sulfonyl group from an activated sulfate donor onto a hydroxyl group (or an amino group, although this is less common) of an acceptor molecule. In eukaryotic cells the activated sulfate donor is 3'-phosphoadenosine-5'-phosphosulfate (PAPS) (Figure 1).
PAPS is synthesized in the cytosol from ATP and sulfate through the sequential action of ATP sulfurylase and APS kinase. ATP sulfurylase first generates adenosine-5'-phosphosulfate (APS) and then APS kinase transfers a phosphate from ATP to APS to create PAPS. The importance of PAPS and sulfation has been discerned in previous studies by using chlorate, an analogue of sulfate, as a competitive inhibitor of ATP sulfurylase. PAPS is a cosubstrate and source of activated sulfate for both cytosolic sulfotransferases and carbohydrate sulfotransferases, which are located in the Golgi. PAPS moves between the cytosol and the Golgi lumen via PAPS/PAP (3’-phosphoadenosine-5’-phosphate) translocase, a transmembrane antiporter.
The exact mechanism used by sulfotransferases is still being elucidated, but studies have indicated that sulfotransferases use an in-line sulfonyl-transfer mechanism that is analogous to the phosphoryl transfer mechanism used by many kinases, which is logical given the great level of structural and functional similarities between kinases and sulfotransferases (Figure 2). In carbohydrate sulfotransferases a conserved lysine has been identified in the active PAPS binding site, which is analogous to a conserved lysine in the active ATP binding site of kinases. Protein sequence alignment studies indicate that this lysine is conserved in cytosolic sulfotransferases as well.
In addition to the conserved lysine, sulfotransferases have a highly conserved histidine in the active site. Based on the conservation of these residues, theoretical models, and experimental measurements a theoretical transition state for catalyzed sulfation has been proposed (Figure 3).
Carbohydrate sulfotransferases are transmembrane enzymes in the Golgi that modify carbohydrates on glycolipids or glyoproteins as they move along the secretory pathway. They have a short cytoplasmic N-terminal, one transmembrane domain, and a large C-terminal Golgi luminal domain. They are distinct from cytosolic sulfotransferases in both structure and function. While cytosolic sulfotransferases play a metabolic role by modifying small molecule substrates such as steroids, flavonoids, neurotransmitters, and phenols, carbohydrate sulfotransferases have a fundamental role in extracellular signalling and adhesion by generating unique ligands through the modification of carbohydrate scaffolds. Since the substrates of carbohydrate sulfotransferases are larger, they have larger active sites than cytosolic sulfotransferases.
Heparan sulfate is a glycosaminoglycan (GAG) that is linked by xylose to serine residues of proteins such as perlecan, syndecan, or glypican. Sulfation of heparan sulfate GAGs helps give diversity to cell surface proteins and provides them with a unique sulfation pattern that allows them to specifically interact with other proteins. For example, in mast cells the AT-III-binding pentasaccharaide is synthesized with essential heparan sulfate sulfation steps. The binding of the heparan sulfate in this pentasaccharide to AT-III inactivates the blood-coagulation factors thrombin and Factor Xa. Heparan sulfates are also known to interact with growth factors, cytokines, chemokines, lipid and membrane binding proteins, and adhesion molecules.
GSTs catalyze sulfation at the 6-hydroxyl group of galactose, N-acetylgalactosamine, or N-acetylglucosamine. Like heparan sulfotransferases, GSTs are responsible for post-translational protein sulfation that assists in cell-signaling. GSTs are also responsible for the sulfation of extracellular matrix (ECM) proteins that assist with maintaining the structure between cells For example, GSTs catalyze the sulfation of glycoproteins displaying the L-selectin binding epitope 6-sulfo sialyl Lewis x, which recruits leukocytes to areas of chronic inflammation. GSTs are also responsible for the proper function of the ECM in the cornea; improper sulfation by GSTs can lead to opaque corneas.
Carbohydrate sulfotransferases are of great interest as drug targets because of their essential roles in cell-cell signalling, adhesion, and ECM maintenance. Their roles in blood coagulation, chronic inflammation, and cornea maintenance mentioned in the Biological Function section above are all of interest for potential therapeutic purposes. In addition to these roles, carbohydrate sulfotransferases are of pharmacological interest because of their roles in viral infection, including herpes simplex virus 1 (HSV-1) and human immunodeficiency virus 1 (HIV-1). Heparan sulfate sites have been shown to be essential for HSV-1 binding that leads to the virus entering the cell. In contrast, heparan sulfate complexes have been shown to bind to HIV-1 and prevent it from entering the cell through its intended target, the CD4 receptor.
Human proteins from this family
- Carbohydrate sulfotransferases 8 (CHST8) and 9 (CHST9), which transfer sulfate to position 4 of non-reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and O-glycans. They function in the biosynthesis of glycoprotein hormones lutropin and thyrotropin, by mediating sulfation of their carbohydrate structures.
- Carbohydrate sulfotransferase 10 (CHST10), which transfers sulfate to position 3 of the terminal glucuronic acid in both protein- and lipid-linked oligosaccharides. It directs the biosynthesis of the HNK-1 carbohydrate structure, a sulfated glucuronyl-lactosaminyl residue carried by many neural recognition molecules, which is involved in cell interactions during ontogenetic development and in synaptic plasticity in the adult.
- Carbohydrate sulfotransferases 11 - 13 (CHST11, CHST12, CHST13), which catalyze the transfer of sulfate to position 4 of the GalNAc residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Some, thought not all, of these enzymes also transfer sulfate to dermatan.
- Carbohydrate sulfotransferase D4ST1 (D4ST1), which transfers sulfate to position 4 of the GalNAc residue of dermatan sulfate.
- Moon, AF.; Edavettal, SC.; Krahn, JM.; Munoz, EM.; Negishi, M.; Linhardt, RJ.; Liu, J.; Pedersen, LC. (Oct 2004). "Structural analysis of the sulfotransferase (3-o-sulfotransferase isoform 3) involved in the biosynthesis of an entry receptor for herpes simplex virus 1". J Biol Chem 279 (43): 45185–93. doi:10.1074/jbc.M405013200. PMID 15304505.
- Nelson, R M; Venot, A; Bevilacqua, M P; Linhardt, R J; Stamenkovic, I (1995). "Carbohydrate-Protein Interactions in Vascular Biology". Annual Review of Cell and Developmental Biology 11 (1): 601–631. doi:10.1146/annurev.cb.11.110195.003125. ISSN 1081-0706.
- Hooper, L.V.; Baenziger, J.U. (1993). "Sulfotransferase and Glycosyltransferase Analyses Using a 96-Well Filtration Plate". Analytical Biochemistry 212 (1): 128–133. doi:10.1006/abio.1993.1301. ISSN 0003-2697. PMID 8368484.
- Bowman, K; Bertozzi, C (1999). "Carbohydrate sulfotransferases: mediators of extracellular communication". Chemistry & Biology 6 (1): R9–R22. doi:10.1016/S1074-5521(99)80014-3. ISSN 1074-5521.
- Klaassen, CD.; Boles, JW. (May 1997). "Sulfation and sulfotransferases 5: the importance of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) in the regulation of sulfation". FASEB J 11 (6): 404–18. PMID 9194521.
- Hemmerich, Stefan (2001). "Carbohydrate sulfotransferases: novel therapeutic targets for inflammation, viral infection and cancer". Drug Discovery Today 6 (1): 27–35. doi:10.1016/S1359-6446(00)01581-6. ISSN 1359-6446. PMID 11165170.
- Baeuerle, PA.; Huttner, WB. (Dec 1986). "Chlorate--a potent inhibitor of protein sulfation in intact cells". Biochem Biophys Res Commun 141 (2): 870–7. doi:10.1016/s0006-291x(86)80253-4. PMID 3026396.
- Ozeran, JD.; Westley, J.; Schwartz, NB. (Mar 1996). "Identification and partial purification of PAPS translocase". Biochemistry 35 (12): 3695–703. doi:10.1021/bi951303m. PMID 8619989.
- Kakuta, Y.; Petrotchenko, EV.; Pedersen, LC.; Negishi, M. (Oct 1998). "The sulfuryl transfer mechanism. Crystal structure of a vanadate complex of estrogen sulfotransferase and mutational analysis". J Biol Chem 273 (42): 27325–30. doi:10.1074/jbc.273.42.27325. PMID 9765259.
- Kamio, K.; Honke, K.; Makita, A. (Dec 1995). "Pyridoxal 5'-phosphate binds to a lysine residue in the adenosine 3'-phosphate 5'-phosphosulfate recognition site of glycolipid sulfotransferase from human renal cancer cells". Glycoconj J 12 (6): 762–6. doi:10.1007/bf00731236. PMID 8748152.
- Sueyoshi, Tatsuya; Kakuta, Yoshimitsu; Pedersen, Lars C.; Wall, Frances E.; Pedersen, Lee G.; Negishi, Masahiko (1998). "A role of Lys614 in the sulfotransferase activity of human heparan sulfate N-deacetylase/N-sulfotransferase". FEBS Letters 433 (3): 211–214. doi:10.1016/S0014-5793(98)00913-2. ISSN 0014-5793. PMID 9744796.
- Chapman, Eli; Best, Michael D.; Hanson, Sarah R.; Wong, Chi-Huey (2004). "Sulfotransferases: Structure, Mechanism, Biological Activity, Inhibition, and Synthetic Utility". Angewandte Chemie International Edition 43 (27): 3526–3548. doi:10.1002/anie.200300631. ISSN 1433-7851.
- Falany, CN. (Mar 1997). "Enzymology of human cytosolic sulfotransferases". FASEB J 11 (4): 206–16. PMID 9068609.
- Shworak, NW.; Liu, J.; Petros, LM.; Zhang, L.; Kobayashi, M.; Copeland, NG.; Jenkins, NA.; Rosenberg, RD. (Feb 1999). "Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. Isolation, characterization, and expression of human cdnas and identification of distinct genomic loci". J Biol Chem 274 (8): 5170–84. doi:10.1074/jbc.274.8.5170. PMID 9988767.
- Hemmerich, S.; Rosen, SD. (Sep 2000). "Carbohydrate sulfotransferases in lymphocyte homing". Glycobiology 10 (9): 849–56. doi:10.1093/glycob/10.9.849. PMID 10988246.
- Rosenberg, RD.; Shworak, NW.; Liu, J.; Schwartz, JJ.; Zhang, L. (May 1997). "Heparan sulfate proteoglycans of the cardiovascular system. Specific structures emerge but how is synthesis regulated?". J Clin Invest 99 (9): 2062–70. doi:10.1172/JCI119377. PMID 9151776.
- Liu, J.; Shworak, NW.; Fritze, LM.; Edelberg, JM.; Rosenberg, RD. (Oct 1996). "Purification of heparan sulfate D-glucosaminyl 3-O-sulfotransferase". J Biol Chem 271 (43): 27072–82. doi:10.1074/jbc.271.43.27072. PMID 8900198.
- Grunwell, Jocelyn R.; Rath, Virginia L.; Rasmussen, Jytte; Cabrilo, Zeljka; Bertozzi, Carolyn R. (2002). "Characterization and Mutagenesis of Gal/GlcNAc-6-O-sulfotransferases†". Biochemistry 41 (52): 15590–15600. doi:10.1021/bi0269557. ISSN 0006-2960. PMID 12501187.
- Shukla, D.; Liu, J.; Blaiklock, P.; Shworak, NW.; Bai, X.; Esko, JD.; Cohen, GH.; Eisenberg, RJ. et al. (Oct 1999). "A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry". Cell 99 (1): 13–22. doi:10.1016/S0092-8674(00)80058-6. PMID 10520990.
- Fukuda M, Hiraoka N, Hindsgaul O, Misra A, Belot F (2001). "R in both N- and O-glycans". Glycobiology 11 (6): –. doi:10.1093/glycob/11.6.495. PMID 11445554.
- Ong E, Fukuda M, Yeh JC, Ding Y, Hindsgaul O (1998). "Expression cloning of a human sulfotransferase that directs the synthesis of the HNK-1 glycan on the neural cell adhesion molecule and glycolipids". J. Biol. Chem. 273 (9): –. doi:10.1074/jbc.273.9.5190. PMID 9478973.
- Ong E, Fukuda M, Fukuda MN, Nakagawa H, Hiraoka N, Akama TO (2000). "Molecular cloning and expression of two distinct human chondroitin 4-O-sulfotransferases that belong to the HNK-1 sulfotransferase gene family". J. Biol. Chem. 275 (26): –. doi:10.1074/jbc.M002443200. PMID 10781601.
- Baenziger JU, Xia G, Evers MR, Kang HG, Schachner M (2001). "Molecular cloning and characterization of a dermatan-specific N-acetylgalactosamine 4-O-sulfotransferase". J. Biol. Chem. 276 (39): –. doi:10.1074/jbc.M105848200. PMID 11470797.
Sulfotransferase family Provide feedback
This family includes a variety of sulfotransferase enzymes. Chondroitin 6-sulfotransferase catalyses the transfer of sulfate to position 6 of the N-acetylgalactosamine residue of chondroitin. This family also includes Heparan sulfate 2-O-sulfotransferase (HS2ST) and Heparan sulfate 6-sulfotransferase (HS6ST). Heparan sulfate (HS) is a co-receptor for a number of growth factors, morphogens, and adhesion proteins. HS biosynthetic modifications may determine the strength and outcome of HS-ligand interactions. Mice that lack HS2ST undergo developmental failure only after midgestation,the most dramatic effect being the complete failure of kidney development . Heparan sulphate 6- O -sulfotransferase (HS6ST) catalyses the transfer of sulphate from adenosine 3'-phosphate, 5'-phosphosulphate to the 6th position of the N -sulphoglucosamine residue in heparan sulphate .
Li J, Shworak NW, Simons M; , J Cell Sci 2002;115:1951-1959.: Increased responsiveness of hypoxic endothelial cells to FGF2 is mediated by HIF-1alpha-dependent regulation of enzymes involved in synthesis of heparan sulfate FGF2-binding sites. PUBMED:11956326 EPMC:11956326
Habuchi H, Miyake G, Nogami K, Kuroiwa A, Matsuda Y, Kusche-Gullberg M, Habuchi O, Tanaka M, Kimata K; , Biochem J 2003;371:131-142.: Biosynthesis of heparan sulphate with diverse structures and functions: two alternatively spliced forms of human heparan sulphate 6-O-sulphotransferase-2 having different expression patterns and properties. PUBMED:12492399 EPMC:12492399
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR005331
This entry consists of a number of carbohydrate sulphotransferases that transfer sulphate to carbohydrate groups in glycoproteins and glycolipids. These include:
- Carbohydrate sulphotransferases 8 and 9, which transfer sulphate to position 4 of non-reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and O-glycans [PUBMED:11445554]. They function in the biosynthesis of glycoprotein hormones lutropin and thyrotropin, by mediating sulphation of their carbohydrate structures.
- Carbohydrate sulphotransferase 10, which transfers sulphate to position 3 of the terminal glucuronic acid in both protein- and lipid-linked oligosaccharides [PUBMED:9478973]. It directs the biosynthesis of the HNK-1 carbohydrate structure, a sulphated glucuronyl-lactosaminyl residue carried by many neural recognition molecules, which is involved in cell interactions during ontogenetic development and in synaptic plasticity in the adult.
- Carbohydrate sulphotransferases 11 - 13, which catalyze the transfer of sulphate to position 4 of the GalNAc residue of chondroitin [PUBMED:10781601]. Chondroitin sulphate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Some, thought not all, of these enzymes also transfer sulphate to dermatan.
- Carbohydrate sulphotransferase D4ST1, which transfers sulphate to position 4 of the GalNAc residue of dermatan sulphate [PUBMED:11470797].
- Heparan sulphate 2-O-sulphotransferase (HS2ST). Heparan sulphate (HS) is a co-receptor for a number of growth factors, morphogens, and adhesion proteins. HS biosynthetic modifications may determine the strength and outcome of HS-ligand interactions. Mice that lack HS2ST undergo developmental failure only after midgestation,the most dramatic effect being the complete failure of kidney development [PUBMED:11956326].
- Heparan-sulphate 6-O-sulphotransferase (HS6ST), which catalyses the transfer of sulphate from adenosine 3'-phosphate, 5'-phosphosulphate to the 6th position of the N -sulphoglucosamine residue in heparan sulphate [PUBMED:12492399].
- Chondroitin 6-sulphotransferase catalyses the transfer of sulphate to position 6 of the N-acetylgalactosamine residue of chondroitin [PUBMED:18697746].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||integral to membrane (GO:0016021)|
|Molecular function||sulfotransferase activity (GO:0008146)|
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AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes .
The clan contains the following 198 members:6PF2K AAA AAA-ATPase_like AAA_10 AAA_11 AAA_12 AAA_13 AAA_14 AAA_15 AAA_16 AAA_17 AAA_18 AAA_19 AAA_2 AAA_21 AAA_22 AAA_23 AAA_24 AAA_25 AAA_26 AAA_27 AAA_28 AAA_29 AAA_3 AAA_30 AAA_31 AAA_32 AAA_33 AAA_34 AAA_35 AAA_4 AAA_5 AAA_6 AAA_7 AAA_8 AAA_9 AAA_PrkA ABC_ATPase ABC_tran ABC_tran_2 Adeno_IVa2 Adenylsucc_synt ADK AFG1_ATPase AIG1 APS_kinase Arch_ATPase Arf ArgK ArsA_ATPase ATP-synt_ab ATP_bind_1 ATP_bind_2 Bac_DnaA CbiA CMS1 CoaE CobA_CobO_BtuR CobU cobW CPT CTP_synth_N Cytidylate_kin Cytidylate_kin2 DAP3 DEAD DEAD_2 DLIC DNA_pack_C DNA_pack_N DNA_pol3_delta DNA_pol3_delta2 DnaB_C dNK DUF1253 DUF1611 DUF2075 DUF2478 DUF258 DUF2791 DUF2813 DUF3584 DUF463 DUF815 DUF853 DUF87 DUF927 Dynamin_N Exonuc_V_gamma FeoB_N Fer4_NifH Flavi_DEAD FTHFS FtsK_SpoIIIE G-alpha Gal-3-0_sulfotr GBP GTP_EFTU GTP_EFTU_D2 GTP_EFTU_D4 Gtr1_RagA Guanylate_kin GvpD HDA2-3 Helicase_C Helicase_C_2 Helicase_C_4 Helicase_RecD Herpes_Helicase Herpes_ori_bp Herpes_TK IIGP IPPT IPT IstB_IS21 KaiC KAP_NTPase Kinesin Kinesin-relat_1 Kinesin-related KTI12 LpxK MCM MEDS Mg_chelatase Mg_chelatase_2 MipZ Miro MMR_HSR1 MobB MukB MutS_V Myosin_head NACHT NB-ARC NOG1 NTPase_1 ParA Parvo_NS1 PAXNEB PduV-EutP PhoH PIF1 Podovirus_Gp16 Polyoma_lg_T_C Pox_A32 PPK2 PPV_E1_C PRK Rad17 Rad51 Ras RecA ResIII RHD3 RHSP RNA12 RNA_helicase RuvB_N SbcCD_C SecA_DEAD Septin Sigma54_activ_2 Sigma54_activat SKI SMC_N SNF2_N Spore_IV_A SRP54 SRPRB Sulfotransfer_1 Sulfotransfer_2 Sulfotransfer_3 Sulphotransf T2SE T4SS-DNA_transf Terminase_1 Terminase_3 Terminase_6 Terminase_GpA Thymidylate_kin TIP49 TK TniB Torsin TraG-D_C tRNA_lig_kinase TrwB_AAD_bind UPF0079 UvrD-helicase UvrD_C UvrD_C_2 Viral_helicase1 VirC1 VirE YhjQ Zeta_toxin Zot
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Curation and family details
|Author:||Finn RD, Bateman A|
|Number in seed:||66|
|Number in full:||2144|
|Average length of the domain:||218.30 aa|
|Average identity of full alignment:||15 %|
|Average coverage of the sequence by the domain:||67.30 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||9|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Sulfotransfer_2 domain has been found. There are 1 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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