Deacetylisoipecoside synthase References Navigation menu4.3.3.3IntEnz viewBRENDA entryNiceZyme viewKEGG...
Histidine ammonia-lyaseFormiminotransferase cyclodeaminaseSerine dehydratasePhenylalanine ammonia-lyaseActive siteBinding siteCatalytic triadOxyanion holeEnzyme promiscuityCatalytically perfect enzymeCoenzymeCofactorEnzyme catalysisEC numberEnzyme superfamilyEnzyme familyList of enzymesOxidoreductaseslistTransferaseslistHydrolaseslistLyaseslistIsomeraseslistLigaseslistTranslocaseslist
EC 4.3.3Enzymes of unknown structure
enzymologyEC4.3.3.3enzymecatalyzeschemical reactionsubstratesH2Oproductsdopaminesecologaninlyasessystematic nameindole and ipecac alkaloid biosynthesis
| deacetylisoipecoside synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.3.3.3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a deacetylisoipecoside synthase (EC 4.3.3.3) is an enzyme that catalyzes the chemical reaction
- deacetylisoipecoside + H2O ⇌{displaystyle rightleftharpoons } dopamine + secologanin
Thus, the two substrates of this enzyme are deacetylisoipecoside and H2O, whereas its two products are dopamine and secologanin.
This enzyme belongs to the family of lyases, specifically amine lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is deacetylisoipecoside dopamine-lyase (secologanin-forming). This enzyme is also called deacetylisoipecoside dopamine-lyase. This enzyme participates in indole and ipecac alkaloid biosynthesis.
References
MH (1997). "Enzymatic condensation of dopamine and secologanin by cell-free extracts of Alangium lamarckii". Phytochemistry. 45 (3): 477–484. doi:10.1016/S0031-9422(96)00828-X..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output .citation q{quotes:"""""""'""'"}.mw-parser-output .citation .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .citation .cs1-lock-limited a,.mw-parser-output .citation .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .citation .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/4/4c/Wikisource-logo.svg/12px-Wikisource-logo.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{font-size:100%}.mw-parser-output .cs1-maint{display:none;color:#33aa33;margin-left:0.3em}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}
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