Enzymes
| UniProtKB help_outline | 3 proteins |
| Enzyme class help_outline |
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Reaction participants Show >> << Hide
- Name help_outline acetyl-CoA Identifier CHEBI:57288 (Beilstein: 8468140) help_outline Charge -4 Formula C23H34N7O17P3S InChIKeyhelp_outline ZSLZBFCDCINBPY-ZSJPKINUSA-J SMILEShelp_outline CC(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 321 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline N-acetylneuraminate Identifier CHEBI:35418 Charge -1 Formula C11H18NO9 InChIKeyhelp_outline SQVRNKJHWKZAKO-LUWBGTNYSA-M SMILEShelp_outline [H][C@]1(OC(O)(C[C@H](O)[C@H]1NC(C)=O)C([O-])=O)[C@H](O)[C@H](O)CO 2D coordinates Mol file for the small molecule Search links Involved in 38 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CoA Identifier CHEBI:57287 (Beilstein: 11604429) help_outline Charge -4 Formula C21H32N7O16P3S InChIKeyhelp_outline RGJOEKWQDUBAIZ-IBOSZNHHSA-J SMILEShelp_outline CC(C)(COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12)[C@@H](O)C(=O)NCCC(=O)NCCS 2D coordinates Mol file for the small molecule Search links Involved in 1,468 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline N-acetyl-9-O-acetylneuraminate Identifier CHEBI:28999 Charge -1 Formula C13H20NO10 InChIKeyhelp_outline NYWZBRWKDRMPAS-GRRZBWEESA-M SMILEShelp_outline [H][C@]1(O[C@@](O)(C[C@H](O)[C@H]1NC(C)=O)C([O-])=O)[C@H](O)[C@H](O)COC(C)=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:26043 | RHEA:26044 | RHEA:26045 | RHEA:26046 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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9-O-Acetylation of sialic acids is catalysed by CASD1 via a covalent acetyl-enzyme intermediate.
Baumann A.M., Bakkers M.J., Buettner F.F., Hartmann M., Grove M., Langereis M.A., de Groot R.J., Muehlenhoff M.
Sialic acids, terminal sugars of glycoproteins and glycolipids, play important roles in development, cellular recognition processes and host-pathogen interactions. A common modification of sialic acids is 9-O-acetylation, which has been implicated in sialoglycan recognition, ganglioside biology, a ... >> More
Sialic acids, terminal sugars of glycoproteins and glycolipids, play important roles in development, cellular recognition processes and host-pathogen interactions. A common modification of sialic acids is 9-O-acetylation, which has been implicated in sialoglycan recognition, ganglioside biology, and the survival and drug resistance of acute lymphoblastic leukaemia cells. Despite many functional implications, the molecular basis of 9-O-acetylation has remained elusive thus far. Following cellular approaches, including selective gene knockout by CRISPR/Cas genome editing, we here show that CASD1--a previously identified human candidate gene--is essential for sialic acid 9-O-acetylation. In vitro assays with the purified N-terminal luminal domain of CASD1 demonstrate transfer of acetyl groups from acetyl-coenzyme A to CMP-activated sialic acid and formation of a covalent acetyl-enzyme intermediate. Our study provides direct evidence that CASD1 is a sialate O-acetyltransferase and serves as key enzyme in the biosynthesis of 9-O-acetylated sialoglycans. << Less
Nat. Commun. 6:7673-7673(2015) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.