Enzymes
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Reaction participants Show >> << Hide
- Name help_outline 5-hydroxyxanthotoxin Identifier CHEBI:78326 Charge -1 Formula C12H7O5 InChIKeyhelp_outline XPFCGZWOHNGDSP-UHFFFAOYSA-M SMILEShelp_outline COc1c2occc2c([O-])c2ccc(=O)oc12 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
- Name help_outline S-adenosyl-L-methionine Identifier CHEBI:59789 Charge 1 Formula C15H23N6O5S InChIKeyhelp_outline MEFKEPWMEQBLKI-AIRLBKTGSA-O SMILEShelp_outline C[S+](CC[C@H]([NH3+])C([O-])=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 842 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline isopimpinellin Identifier CHEBI:28853 (Beilstein: 262337; CAS: 482-27-9) help_outline Charge 0 Formula C13H10O5 InChIKeyhelp_outline DFMAXQKDIGCMTL-UHFFFAOYSA-N SMILEShelp_outline COc1c2ccoc2c(OC)c2oc(=O)ccc12 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline S-adenosyl-L-homocysteine Identifier CHEBI:57856 Charge 0 Formula C14H20N6O5S InChIKeyhelp_outline ZJUKTBDSGOFHSH-WFMPWKQPSA-N SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](CSCC[C@H]([NH3+])C([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 768 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:24894 | RHEA:24895 | RHEA:24896 | RHEA:24897 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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The molecular and structural basis of O-methylation reaction in coumarin biosynthesis in Peucedanum praeruptorum Dunn.
Zhao Y., Wang N., Sui Z., Huang C., Zeng Z., Kong L.
Methoxylated coumarins represent a large proportion of officinal value coumarins while only one enzyme specific to bergaptol <i>O</i>-methylation (BMT) has been identified to date. The multiple types of methoxylated coumarins indicate that at least one unknown enzyme participates in the <i>O</i>-m ... >> More
Methoxylated coumarins represent a large proportion of officinal value coumarins while only one enzyme specific to bergaptol <i>O</i>-methylation (BMT) has been identified to date. The multiple types of methoxylated coumarins indicate that at least one unknown enzyme participates in the <i>O</i>-methylation of other hydroxylated coumarins and remains to be identified. Combined transcriptome and metabonomics analysis revealed that an enzyme similar to caffeic acid <i>O</i>-methyltransferase (COMT-S, S is short for similar) was involved in catalyzing all the hydroxylated coumarins in <i>Peucedanum praeruptorum</i>. However, the precise molecular mechanism of its substrate heterozygosis remains unsolved. Pursuing this question, we determined the crystal structure of COMT-S to clarify its substrate preference. The result revealed that Asn132, Asp271, and Asn325 govern the substrate heterozygosis of COMT-S. A single mutation, such as N132A, determines the catalytic selectivity of hydroxyl groups in esculetin and also causes production differences in bergapten. Evolution-based analysis indicated that BMT was only recently derived as a paralogue of caffeic acid <i>O</i>-methyltransferase (COMT) via gene duplication, occurring before the Apiaceae family divergence between 37 and 100 mya. The present study identified the previously unknown <i>O</i>-methylation steps in coumarin biosynthesis. The crystallographic and mutational studies provided a deeper understanding of the substrate preference, which can be used for producing specific <i>O</i>-methylation coumarins. Moreover, the evolutionary relationship between BMT and COMT-S was clarified to facilitate understanding of evolutionary events in the Apiaceae family. << Less
Int. J. Mol. Sci. 20:0-0(2019) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.
Comments
Published in: "Elicitor-stimulated furanocoumarin biosynthesis in cultured parsley cells - S-adenosyl-L-methionine-bergaptol and S-adenosyl-L-methionine-xanthotoxol O-methyltransferases." Hauffe, K.D., Hahlbrock, K. and Scheel, D. https://doi.org/10.1515/znc-1986-1-234