3,4-dihydroxy-5-polyprenylbenzoic acid O-methyltransferase activity [GO_0010420]
Catalysis of the reaction: 3,4-dihydroxy-5-polyprenylbenzoic acid + S-adenosyl-L-methionine = 3-methoxy-4-hydroxy-5-polyprenylbenzoic acid + S-adenosyl-L-homocysteine + H+. Note that the polyprenyl sidechain substrate for this reaction has a different number of prenyl units in different organisms (for example, ubiquinone-6 in Saccharomyces, ubiquinone- 9 in rat and ubiquinone-10 in human), and thus the natural substrate for the enzymes from different organisms has a different number of prenyl units. However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units.
Note
This page displays the raw VFB json record for this term. Please use the link below to open the term inside the Virtual Fly Brain viewerOpen 3,4-dihydroxy-5-polyprenylbenzoic acid O-methyltransferase activity in VFB
Term Information
- ID: GO_0010420
- Name: 3,4-dihydroxy-5-polyprenylbenzoic acid O-methyltransferase activity
- Definition: Catalysis of the reaction: 3,4-dihydroxy-5-polyprenylbenzoic acid + S-adenosyl-L-methionine = 3-methoxy-4-hydroxy-5-polyprenylbenzoic acid + S-adenosyl-L-homocysteine + H+.
- Synonyms:
- Type:
- Comment: Note that the polyprenyl sidechain substrate for this reaction has a different number of prenyl units in different organisms (for example, ubiquinone-6 in Saccharomyces, ubiquinone- 9 in rat and ubiquinone-10 in human), and thus the natural substrate for the enzymes from different organisms has a different number of prenyl units. However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units.
VFB Term Json
{
"term": {
"core": {
"iri": "http://purl.obolibrary.org/obo/GO_0010420",
"symbol": "",
"types": [
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],
"short_form": "GO_0010420",
"unique_facets": [
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],
"label": "3,4-dihydroxy-5-polyprenylbenzoic acid O-methyltransferase activity"
},
"description": [
"Catalysis of the reaction: 3,4-dihydroxy-5-polyprenylbenzoic acid + S-adenosyl-L-methionine = 3-methoxy-4-hydroxy-5-polyprenylbenzoic acid + S-adenosyl-L-homocysteine + H+."
],
"comment": [
"Note that the polyprenyl sidechain substrate for this reaction has a different number of prenyl units in different organisms (for example, ubiquinone-6 in Saccharomyces, ubiquinone- 9 in rat and ubiquinone-10 in human), and thus the natural substrate for the enzymes from different organisms has a different number of prenyl units. However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units."
]
},
"query": "Get JSON for Class",
"version": "275438e",
"parents": [
{
"symbol": "",
"iri": "http://purl.obolibrary.org/obo/GO_0008757",
"types": [
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],
"short_form": "GO_0008757",
"unique_facets": [
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],
"label": "S-adenosylmethionine-dependent methyltransferase activity"
}
],
"relationships": [
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"relation": {
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"label": "is part of",
"type": "part_of"
},
"object": {
"symbol": "",
"iri": "http://purl.obolibrary.org/obo/GO_0006744",
"types": [
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"short_form": "GO_0006744",
"unique_facets": [
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],
"label": "ubiquinone biosynthetic process"
}
}
],
"xrefs": [],
"anatomy_channel_image": [],
"pub_syn": [
{
"synonym": {
"scope": "has_related_synonym",
"label": "polyprenyldihydroxybenzoate methyltransferase activity",
"type": ""
},
"pub": {
"core": {
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"iri": "http://flybase.org/reports/Unattributed",
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"short_form": "Unattributed",
"unique_facets": [
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"label": ""
},
"FlyBase": "",
"PubMed": "",
"DOI": ""
}
}
],
"def_pubs": []
}
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