| Entry |
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| Name |
polyprenyldihydroxybenzoate methyltransferase;
3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase;
dihydroxyhexaprenylbenzoate methyltransferase;
COQ3 (gene name);
Coq3 O-methyltransferase;
DHHB O-methyltransferase
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| Class |
Transferases;
Transferring one-carbon groups;
Methyltransferases
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| Sysname |
S-adenosyl-L-methionine:3,4-dihydroxy-5-all-trans-polyprenylbenzoate 3-O-methyltransferase
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| Reaction(IUBMB) |
S-adenosyl-L-methionine + 3,4-dihydroxy-5-all-trans-polyprenylbenzoate = S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-all-trans-polyprenylbenzoate [RN: R08771]
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| Reaction(KEGG) |
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| Substrate |
S-adenosyl-L-methionine [CPD: C00019];
3,4-dihydroxy-5-all-trans-polyprenylbenzoate
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| Product |
S-adenosyl-L-homocysteine [CPD: C00021];
3-methoxy-4-hydroxy-5-all-trans-polyprenylbenzoate
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| Comment |
This enzyme is involved in ubiquinone biosynthesis. Ubiquinones from different organisms have a different number of prenyl units (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. For example, the human COQ3 enzyme can restore biosynthesis of ubiquinone-6 in coq3 deletion mutants of yeast [3]. The enzymes from yeast and rat also catalyse the methylation of 3-demethylubiquinol-6 and 3-demethylubiquinol-9, respectively [2] (this activity is classified as EC 2.1.1.64, 3-demethylubiquinol 3-O-methyltransferase).
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| History |
EC 2.1.1.114 created 1999
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| Pathway |
| Ubiquinone and other terpenoid-quinone biosynthesis | | Metabolic pathways | | Biosynthesis of secondary metabolites |
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| Orthology |
| polyprenyldihydroxybenzoate methyltransferase / 3-demethylubiquinol 3-O-methyltransferase |
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| Genes |
HSA: | | PTR: | | PPS: | | GGO: | | PON: | | NLE: | | MCC: | | MCF: | | CSAB: | | RRO: | | CJC: | | SBQ: | | MMU: | | RNO: | | CGE: | | NGI: | | HGL: | | CCAN: | | OCU: | | TUP: | | CFA: | | AML: | | UMR: | | FCA: | | PTG: | | AJU: | | BTA: | | BOM: | | BIU: | | PHD: | | CHX: | | OAS: | | SSC: | | CFR: | | BACU: | | LVE: | | ECB: | | MYB: | | MYD: | | HAI: | | RSS: | | PALE: | | LAV: | | MDO: | | SHR: | | OAA: | | GGA: | | MGP: | | CJO: | | APLA: | | ACYG: | | TGU: | | GFR: | | FAB: | | PHI: | | CCW: | | FPG: | | FCH: | | CLV: | | AAM: | | ASN: | | AMJ: | | PSS: | | CMY: | | CPIC: | | ACS: | | PBI: | | GJA: | | XLA: | | XTR: | | NPR: | | DRE: | | SRX: | | SANH: | | SGH: | | IPU: | | TRU: | | TNG: | | LCO: | | NCC: | | MZE: | | OLA: | | XMA: | | CSEM: | | LCF: | | SASA: | | ELS: | | SFM: | | LCM: | | CMK: | | BFO: | | CIN: | | SPU: | | SKO: | | DME: | | DPO: | | DAN: | | DER: | | DPE: | | DSE: | | DSI: | | DWI: | | DYA: | | DGR: | | DMO: | | DVI: | | MDE: | | AGA: | | AAG: | | CQU: | | AME: | | BIM: | | BTER: | | SOC: | | AEC: | | ACEP: | | PBAR: | | HST: | | CFO: | | LHU: | | NVI: | | TCA: | | DPA: | | NVL: | | BMOR: | | PXY: | | API: | | DNX: | | PHU: | | DPX: | | ISC: | | TUT: | | CEL: | | CBR: | | BMY: | | LOA: | | TSP: | | HRO: | | LGI: | | CRG: | | OBI: | | SMM: | | OVI: | | NVE: | | ADF: | | HMG: | | TAD: | | AQU: | | ATH: | | ALY: | | CRB: | | EUS: | | BRP: | | BNA: | | THJ: | | CIT: | | CIC: | | TCC: | | GRA: | | GHI: | | GMX: | | VRA: | | VAR: | | CCAJ: | | MTR: | | CAM: | | ADU: | | AIP: | | FVE: | | PPER: | | PMUM: | | MDM: | | PXB: | | ZJU: | | CMO: | | JCU: | | POP: | | SIND: | | BVG: | | NNU: | | OSA: | | DOSA: | | OBR: | | SBI: | | ZMA: | | SITA: | | EGU: | | SCE: | | AGO: | | ERC: | | KLA: | | LTH: | | VPO: | | ZRO: | | CGR: | | NCS: | | NDI: | | TPF: | | TBL: | | TDL: | | KAF: | | PPA: | | DHA: | | PIC: | | PGU: | | SPAA: | | LEL: | | CAL: | | CTP: | | COT: | | CDU: | | CTEN: | | YLI: | | CLU: | | CAUR: | | DDI: | | DPP: | | DFA: | | TAN: | | TPV: | | TOT: | | BEQ: | | CPV: | | CHO: | | TET: | | PTM: | |
» show all
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| Reference |
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| Authors |
Clarke CF, Williams W, Teruya JH. |
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| Title |
Ubiquinone biosynthesis in Saccharomyces cerevisiae. Isolation and sequence of COQ3, the 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase gene. |
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| Journal |
J. Biol. Chem. 266 (1991) 16636-44. |
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| Sequence |
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| Reference |
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| Authors |
Poon WW, Barkovich RJ, Hsu AY, Frankel A, Lee PT, Shepherd JN, Myles DC, Clarke CF |
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| Title |
Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis. |
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| Journal |
J. Biol. Chem. 274 (1999) 21665-72. |
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| Sequence |
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| Reference |
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| Authors |
Jonassen T, Clarke CF |
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| Title |
Isolation and functional expression of human COQ3, a gene encoding a methyltransferase required for ubiquinone biosynthesis. |
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| Journal |
J. Biol. Chem. 275 (2000) 12381-7. |
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| Sequence |
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| Reference |
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| Authors |
Xing L, Zhu Y, Fang P, Wang J, Zeng F, Li X, Teng M, Li X |
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| Title |
Crystallization and preliminary crystallographic studies of UbiG, an O-methyltransferase from Escherichia coli. |
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| Journal |
Acta. Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. 67 (2011) 727-9. |
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| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: CAS: 139569-31-6 |
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| LinkDB |
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