Enzymes
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- Name help_outline 3',4',5-trihydroxy-3,7-dimethoxyflavone Identifier CHEBI:77710 Charge -1 Formula C17H13O7 InChIKeyhelp_outline LUJAXSNNYBCFEE-UHFFFAOYSA-M SMILEShelp_outline COc1cc([O-])c2c(c1)oc(-c1ccc(O)c(O)c1)c(OC)c2=O 2D coordinates Mol file for the small molecule Search links Involved in 3 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 3',5-dihydroxy-3,4',7-trimethoxyflavone Identifier CHEBI:77770 Charge -1 Formula C18H15O7 InChIKeyhelp_outline KPCRYSMUMBNTCK-UHFFFAOYSA-M SMILEShelp_outline COc1cc([O-])c2c(c1)oc(-c1ccc(OC)c(O)c1)c(OC)c2=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
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 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:21832 | RHEA:21833 | RHEA:21834 | RHEA:21835 | |
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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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Enzymatic synthesis of polymethylated flavonols in Chrysosplenium americanum. II. Substrate interaction and product inhibition studies of flavonol 3-, 6-, and 4'-O-methyltransferases.
De Luca V., Ibrahim R.K.
The steady-state kinetic behavior of three position-specific O-methyltransferases (3-, 4'-, and 6-OMTs) was compared with reference to substrate inhibition patterns in Chrysosplenium americanum. The 6-OMT was severely inhibited by the flavonoid substrate at concentrations close to Km, whereas the ... >> More
The steady-state kinetic behavior of three position-specific O-methyltransferases (3-, 4'-, and 6-OMTs) was compared with reference to substrate inhibition patterns in Chrysosplenium americanum. The 6-OMT was severely inhibited by the flavonoid substrate at concentrations close to Km, whereas the other two enzymes were less affected by their respective flavonoid substrates. Substrate interaction kinetics for the 6-OMT gave converging lines consistent with a sequential binding mechanism, whereas the data generated for the 3- and 4'-OMTs could be fitted to the equation for a ping-pong mechanism or to that of a sequential binding mechanism where Kia was much smaller Ka. More information on the mechanism of reaction was obtained from product inhibition studies. The three enzymes exhibited competitive inhibition patterns between S-adenosyl-L-methionine (SAM) and S-adenosyl-L-homocysteine (SAH), whereas other patterns were either noncompetitive or uncompetitive. The steady-state kinetic properties of the 3-, 4'-, and 6-OMTs were consistent with a sequential ordered reaction mechanism, in which SAM and SAH were leading reaction partners and included an abortive EQB complex. Product inhibition constants were sufficiently low to suggest that these may be important in regulating the pathway of polymethylated flavonoid synthesis. It was suggested that due to their greater sensitivity to inhibition by SAH, the OMTs involved in earlier steps of the methylation sequence may regulate the rate of synthesis of final products in Chrysosplenium. << Less
Arch Biochem Biophys 238:606-618(1985) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Enzymatic synthesis of polymethylated flavonols in Chrysosplenium americanum. I. Partial purification and some properties of S-adenosyl-L-methionine:flavonol 3-, 6-, 7-, and 4'-O-methyltransferases.
De Luca V., Ibrahim R.K.
Four novel flavonol O-methyltransferases (OMTs) were partially purified from Chrysosplenium americanum by precipitation with ammonium sulfate, successive chromatography on Sephacryl S-200 and hydroxylapatite, and chromatofocusing on Polybuffer ion exchanger. They exhibited strict position specific ... >> More
Four novel flavonol O-methyltransferases (OMTs) were partially purified from Chrysosplenium americanum by precipitation with ammonium sulfate, successive chromatography on Sephacryl S-200 and hydroxylapatite, and chromatofocusing on Polybuffer ion exchanger. They exhibited strict position specificity for positions 3 of quercetin, 7 of 3-methylquercetin, 4' of 3,7-dimethylquercetin, and 6 of 3,7,3'-trimethylquercetagetin. None of these enzymes reacted with phenylpropanoids, flavones, dihydroflavonols, or any of their glucosides. Except for the 7-OMT whose activity was lost during chromatofocusing, the other enzymes had apparent pI values of 4.8, 5.4, and 5.7 for the 3-, 4'-, and 6-OMTs, respectively. They had similar molecular weights (Mr 57,000) and their pH optima varied between 7.8 and 9.0, with a shift in optimal activity from lower to higher pH with increasing level of substrate methylation. Unlike the 3 and 4' enzymes, the 6-OMT showed an absolute requirement for Mg2+ whose activation was saturable and was inhibited by EDTA. The in vitro stepwise O-methylation of quercetin----3-methylquercetin----3,7-dimethylquercetin----3 ,7, 4'-trimethylquercetin tends to suggest a coordinated sequence of methyl transfers in this tissue. << Less
Arch Biochem Biophys 238:596-605(1985) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.