Enzymes
| UniProtKB help_outline | 5 proteins |
| Enzyme class help_outline |
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Reaction participants Show >> << Hide
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Name help_outline
4-hydroxy-3-all-trans-polyprenylbenzoate
Identifier
CHEBI:78396
Charge
-1
Formula
(C5H8)nC7H5O3
Search links
Involved in 18 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:9514Polymer name: a 4-hydroxy-3-(all-trans-polyprenyl)benzoatePolymerization index help_outline nFormula C7H5O3(C5H8)nCharge (-1)(0)nMol File for the polymer
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Namehelp_outline
reduced [2Fe-2S]-[ferredoxin]
Identifier
RHEA-COMP:10001
Reactive part
help_outline
- Name help_outline [2Fe-2S]1+ Identifier CHEBI:33738 Charge 1 Formula Fe2S2 InChIKeyhelp_outline MAGIRAZQQVQNKP-UHFFFAOYSA-N SMILEShelp_outline S1[Fe]S[Fe+]1 2D coordinates Mol file for the small molecule Search links Involved in 263 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline O2 Identifier CHEBI:15379 (CAS: 7782-44-7) help_outline Charge 0 Formula O2 InChIKeyhelp_outline MYMOFIZGZYHOMD-UHFFFAOYSA-N SMILEShelp_outline O=O 2D coordinates Mol file for the small molecule Search links Involved in 2,851 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 9,932 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Name help_outline
3,4-dihydroxy-5-all-trans-polyprenylbenzoate
Identifier
CHEBI:64694
Charge
-1
Formula
C7H5O4(C5H8)n
Search links
Involved in 13 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:10930Polymer name: a 3,4-dihydroxy-5-(all-trans-polyprenyl)benzoatePolymerization index help_outline nFormula C7H5O4(C5H8)nCharge (-1)(0)nMol File for the polymer
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Namehelp_outline
oxidized [2Fe-2S]-[ferredoxin]
Identifier
RHEA-COMP:10000
Reactive part
help_outline
- Name help_outline [2Fe-2S]2+ Identifier CHEBI:33737 Charge 2 Formula Fe2S2 InChIKeyhelp_outline XSOVBBGAMBLACL-UHFFFAOYSA-N SMILEShelp_outline S1[Fe+]S[Fe+]1 2D coordinates Mol file for the small molecule Search links Involved in 263 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,485 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:81195 | RHEA:81196 | RHEA:81197 | RHEA:81198 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
Specific form(s) of this reaction
Publications
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In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis.
Nicoll C.R., Alvigini L., Gottinger A., Cecchini D., Mannucci B., Corana F., Mascotti M.L., Mattevi A.
Metabolons are protein assemblies that perform a series of reactions in a metabolic pathway. However, the general importance and aptitude of metabolons for enzyme catalysis remain poorly understood. In animals, biosynthesis of coenzyme Q is currently attributed to ten different proteins, with COQ3 ... >> More
Metabolons are protein assemblies that perform a series of reactions in a metabolic pathway. However, the general importance and aptitude of metabolons for enzyme catalysis remain poorly understood. In animals, biosynthesis of coenzyme Q is currently attributed to ten different proteins, with COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9 forming the iconic COQ metabolon. Yet several reaction steps conducted by the metabolon remain enigmatic. To elucidate the prerequisites for animal coenzyme Q biosynthesis, we sought to construct the entire metabolon in vitro. Here we show that this approach, rooted in ancestral sequence reconstruction, reveals the enzymes responsible for the uncharacterized steps and captures the biosynthetic pathway in vitro. We demonstrate that COQ8, a kinase, increases and streamlines coenzyme Q production. Our findings provide crucial insight into how biocatalytic efficiency is regulated and enhanced by these biosynthetic engines in the context of the cell. << Less
Nat. Catal. 7:148-160(2024) [PubMed] [EuropePMC]
This publication is cited by 25 other entries.