Human Metabolome Database: Showing metabocard for Coenzyme Q10 (HMDB0001072)

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Identification Taxonomy Ontology Physical properties Spectra Biological properties Concentrations Links References enzymes (17) Show 17 proteins XML

enzymes (17) Show 17 proteins

Record Information

Version

4.0

Status

Detected and Quantified

Creation Date

2005-11-16 15:48:42 UTC

Update Date

2018-05-20 08:58:20 UTC

HMDB ID

HMDB0001072

Secondary Accession Numbers

HMDB01072

Metabolite Identification

Common Name

Coenzyme Q10

Description

Coenzyme Q10 (ubiquinone) is a naturally occurring compound widely distributed in animal organisms and in humans. The primary compounds involved in the biosynthesis of ubiquinone are 4-hydroxybenzoate and the polyprenyl chain. An essential role of coenzyme Q10 is as an electron carrier in the mitochondrial respiratory chain. Moreover, coenzyme Q10 is one of the most important lipophilic antioxidants, preventing the generation of free radicals as well as oxidative modifications of proteins, lipids, and DNA, it and can also regenerate the other powerful lipophilic antioxidant, alpha-tocopherol. Antioxidant action is a property of the reduced form of coenzyme Q10, ubiquinol (CoQ10H2), and the ubisemiquinone radical (CoQ10H*). Paradoxically, independently of the known antioxidant properties of coenzyme Q10, the ubisemiquinone radical anion (CoQ10-) possesses prooxidative properties. Decreased levels of coenzyme Q10 in humans are observed in many pathologies (e.g. cardiac disorders, neurodegenerative diseases, AIDS, cancer) associated with intensive generation of free radicals and their action on cells and tissues. In these cases, treatment involves pharmaceutical supplementation or increased consumption of coenzyme Q10 with meals as well as treatment with suitable chemical compounds (i.e. folic acid or B-group vitamins) which significantly increase ubiquinone biosynthesis in the organism. Estimation of coenzyme Q10 deficiency and efficiency of its supplementation requires a determination of ubiquinone levels in the organism. Therefore, highly selective and sensitive methods must be applied, such as HPLC with UV or coulometric detection. For a number of years, coenzyme Q (CoQ10 in humans) was known for its key role in mitochondrial bioenergetics; later studies demonstrated its presence in other subcellular fractions and in plasma, and extensively investigated its antioxidant role. These two functions constitute the basis on which research supporting the clinical use of CoQ10 is founded. Also at the inner mitochondrial membrane level, coenzyme Q is recognized as an obligatory co-factor for the function of uncoupling proteins and a modulator of the transition pore. Furthermore, recent data reveal that CoQ10 affects expression of genes involved in human cell signalling, metabolism, and transport and some of the effects of exogenously administered CoQ10 may be due to this property. Coenzyme Q is the only lipid soluble antioxidant synthesized endogenously. In its reduced form, CoQH2, ubiquinol, inhibits protein and DNA oxidation but it is the effect on lipid peroxidation that has been most deeply studied. Ubiquinol inhibits the peroxidation of cell membrane lipids and also that of lipoprotein lipids present in the circulation. Dietary supplementation with CoQ10 results in increased levels of ubiquinol-10 within circulating lipoproteins and increased resistance of human low-density lipoproteins to the initiation of lipid peroxidation. Moreover, CoQ10 has a direct anti-atherogenic effect, which has been demonstrated in apolipoprotein E-deficient mice fed with a high-fat diet. (PMID: 15928598 , 17914161 ).

Structure

MOL SDF PDB SMILES InChI

Synonyms

Value	Source
2-((all-e)-3,7,11,15,19,23,27,31,35,39-Decamethyl-2,6,10,14,18,22,26,30,34,38-tetracontadecaenyl)-5,6-dimethoxy-3-methyl-P-benzoquinone	ChEBI
2-[(2E,6E,10E,14E,18E,22E,26E,30E,34E)-3,7,11,15,19,23,27,31,35,39-Decamethyltetraconta-2,6,10,14,18,22,26,30,34,38-decaen-1-yl]-5,6-dimethoxy-3-methyl-1,4-benzoquinone	ChEBI
Adelir	ChEBI
all-trans-Ubiquinone	ChEBI
CoQ	ChEBI
CoQ10	ChEBI
Q	ChEBI
Q 199	ChEBI
Q10	ChEBI
Ubidecarenone	ChEBI
Ubiquinone	ChEBI
Ubiquinone 10	ChEBI
Ubiquinone 50	ChEBI
UBIQUINONE-10	ChEBI
(all-e)-2,3-Dimethoxy-5-methyl-6-(3,7,11,15,19,23,27,31-octamethyl-2,6,10,14,18,22,26,30-dotriacontaoctaenyl)-2,5-cyclohexadiene-1,4-dione	HMDB
(all-e)-2-(3,7,11,15,19,23,27,31,35,39-Decamethyl-2,6,10,14,18,22,26,30,34,38-tetracontadecaenyl)-5,6-dimethoxy-3-methyl-2,5-cyclohexadiene-1,4-dione	HMDB
2-(3,7,11,15,19,23,27,31,35,39-Decamethyl-2,6,10,14,18,22,26,30,34,38-tetracontadecaenyl)-5,6-dimethoxy-3-methyl-P-benzoquinone	HMDB
2-[(2E,6E,10E,14E,18E,22E,26E,30E,34E)-3,7,11,15,19,23,27,31,35,39-Decamethyl-2,6,10,14,18,22,26,30,34,38-tetracontadecaenyl]-5,6-dimethoxy-3-methyl- 2,5-cyclohexadiene-1,4-dione	HMDB
4-Ethyl-5-fluoropyrimidine	HMDB
Aqua Q 10l10	HMDB
Aqua Q10	HMDB
bio-Quinon	HMDB
bio-Quinone Q10	HMDB
Ensorb	HMDB
Kaneka Q10	HMDB
Kudesan	HMDB
Li-Q-sorb	HMDB
Liquid-Q	HMDB
Neuquinon	HMDB
Neuquinone	HMDB
PureSorb Q 40	HMDB
Q 10AA	HMDB
Q-Gel	HMDB
Q-Gel 100	HMDB
Ubiquinone Q10	HMDB
Unbiquinone	HMDB
Unispheres Q 10	HMDB
2,3-Dimethoxy-5-methyl-6-decaprenylbenzoquinone	MeSH
CO-Enzyme Q10	MeSH
Ubisemiquinone	MeSH
CoQ 10	MeSH
Q-Ter	MeSH
Coenzyme Q10, (Z,Z,Z,Z,Z,Z,e,e,e)-isomer	MeSH
Coenzyme Q10, ion (1-), (all-e)-isomer	MeSH
Ubisemiquinone radical	MeSH

Chemical Formula

C₅₉H₉₀O₄

Average Molecular Weight

863.3435

Monoisotopic Molecular Weight

862.683911368

IUPAC Name

2-[(2E,6E,10E,14E,18E,22E,26E,30E,34E)-3,7,11,15,19,23,27,31,35,39-decamethyltetraconta-2,6,10,14,18,22,26,30,34,38-decaen-1-yl]-5,6-dimethoxy-3-methylcyclohexa-2,5-diene-1,4-dione

Traditional Name

coenzyme-Q10

CAS Registry Number

303-98-0

SMILES

COC1=C(OC)C(=O)C(C\C=C(/C)CC\C=C(/C)CC\C=C(/C)CC\C=C(/C)CC\C=C(/C)CC\C=C(/C)CC\C=C(/C)CC\C=C(/C)CC\C=C(/C)CCC=C(C)C)=C(C)C1=O

InChI Identifier

InChI=1S/C59H90O4/c1-44(2)24-15-25-45(3)26-16-27-46(4)28-17-29-47(5)30-18-31-48(6)32-19-33-49(7)34-20-35-50(8)36-21-37-51(9)38-22-39-52(10)40-23-41-53(11)42-43-55-54(12)56(60)58(62-13)59(63-14)57(55)61/h24,26,28,30,32,34,36,38,40,42H,15-23,25,27,29,31,33,35,37,39,41,43H2,1-14H3/b45-26+,46-28+,47-30+,48-32+,49-34+,50-36+,51-38+,52-40+,53-42+

InChI Key

ACTIUHUUMQJHFO-UPTCCGCDSA-N

Chemical Taxonomy

Description

This compound belongs to the class of organic compounds known as ubiquinones. These are coenzyme Q derivatives containing a 5, 6-dimethoxy-3-methyl(1,4-benzoquinone) moiety to which an isoprenyl group is attached at ring position 2(or 6).

Kingdom

Organic compounds

Super Class

Lipids and lipid-like molecules

Class

Prenol lipids

Sub Class

Quinone and hydroquinone lipids

Direct Parent

Ubiquinones

Alternative Parents

Substituents

Polyterpenoid
Polyprenylbenzoquinone
Ubiquinone skeleton
Quinone
P-benzoquinone
Vinylogous ester
Cyclic ketone
Ketone
Organic oxygen compound
Organic oxide
Hydrocarbon derivative
Organooxygen compound
Carbonyl group
Aliphatic homomonocyclic compound

Molecular Framework

Aliphatic homomonocyclic compounds

External Descriptors

ubiquinones (CHEBI:46245 )
ubiquinones (C11378 )
Coenzymes (C11378 )
Ubiquinones (LMPR02010001 )

Ontology

Disposition

Route of exposure:

Enteral:

Ingestion

Source:

Biological location:

Cell and elements:

Extracellular

Organ and components:

Tissue and substructures:

Biofluid and excreta:

Blood

Subcellular:

Process

Naturally occurring process:

Biological process:

Biochemical process:

Chemical reaction:

Lipid peroxidation

Cellular process:

Cell signaling

Biochemical pathway:

Role

Industrial application:

Pharmaceutical industry:

Pharmaceutical

Biological role:

Physical Properties

State

Solid

Experimental Properties

Property	Value	Reference
Melting Point	Not Available	Not Available
Boiling Point	Not Available	Not Available
Water Solubility	Not Available	Not Available
LogP	Not Available	Not Available

Predicted Properties

Property	Value	Source
Water Solubility	0.00019 g/L	ALOGPS
logP	9.94	ALOGPS
logP	17.16	ChemAxon
logS	-6.6	ALOGPS
pKa (Strongest Basic)	-4.7	ChemAxon
Physiological Charge	0	ChemAxon
Hydrogen Acceptor Count	4	ChemAxon
Hydrogen Donor Count	0	ChemAxon
Polar Surface Area	52.6 Å²	ChemAxon
Rotatable Bond Count	31	ChemAxon
Refractivity	286.61 m³·mol⁻¹	ChemAxon
Polarizability	112.38 Å³	ChemAxon
Number of Rings	1	ChemAxon
Bioavailability	0	ChemAxon
Rule of Five	Yes	ChemAxon
Ghose Filter	Yes	ChemAxon
Veber's Rule	Yes	ChemAxon
MDDR-like Rule	Yes	ChemAxon

Spectra

Spectrum Type	Description	Splash Key
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 10V, Positive	splash10-03dj-0211111090-6a869102747ec5ae93a4	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 20V, Positive	splash10-00kb-1859498220-7339f4669211f439f21a	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 40V, Positive	splash10-00kb-2131239600-0459da83925ec9d0e79f	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 10V, Negative	splash10-03di-0000000090-b50a0138d910d6641b72	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 20V, Negative	splash10-08i4-0000000890-33ee289015ac39ff3df8	View in MoNA
Predicted LC-MS/MS	Predicted LC-MS/MS Spectrum - 40V, Negative	splash10-000b-3000000940-d7a250f754c937cceb37	View in MoNA

Biological Properties

Cellular Locations

Cytoplasm
Extracellular
Membrane (predicted from logP)
Mitochondria

Biospecimen Locations

Blood
Feces

Tissue Location

Brain
Kidney
Liver
Lymphocyte
Muscle
Skeletal Muscle

Pathways

Name	SMPDB/Pathwhiz	KEGG
Mitochondrial Electron Transport Chain
Citric Acid Cycle
Congenital lactic acidosis		Not Available
Fumarase deficiency		Not Available
Mitochondrial complex II deficiency		Not Available

Normal Concentrations

Biospecimen	Status	Value	Age	Sex	Condition	Reference	Details
Blood	Detected and Quantified	1.17 +/- 0.12 uM	Adult (>18 years old)	Male	Normal	Geigy Scientific ...	details
Blood	Detected and Quantified	0.65 +/- 0.18 uM	Adult (>18 years old)	Female	Normal	Geigy Scientific ...	details
Blood	Detected and Quantified	0.85 (0.46-1.33) uM	Adult (>18 years old)	Both	Normal	Geigy Scientific ...	details
Blood	Detected and Quantified	0.040 +/- 0.014 uM	Adult (>18 years old)	Male	Normal	16583456	details
Blood	Detected and Quantified	0.056 +/- 0.023 uM	Adult (>18 years old)	Male	Normal	16583456	details
Blood	Detected and Quantified	4.31 +/- 0.42 uM	Adult (>18 years old)	Both	Normal	20671299	details

Abnormal Concentrations

Biospecimen	Status	Value	Age	Sex	Condition	Reference	Details
Feces	Detected but not Quantified		Newborn (0-30 days old)	Not Specified	Premature neonates	23210743	details

Associated Disorders and Diseases

Disease References

None

Associated OMIM IDs

None

External Links

DrugBank ID

DB09270

Phenol Explorer Compound ID

Not Available

FoodDB ID

KNApSAcK ID

Chemspider ID

KEGG Compound ID

BioCyc ID

BiGG ID

Wikipedia Link

METLIN ID

PubChem Compound

PDB ID

ChEBI ID

References

Synthesis Reference

Seo, Myung-Ji; Im, Eun-Mi; Hur, Jin-Haeng; Nam, Jung-Yeon; Hyun, Chang-Gu; Pyun, Yu-Ryang; Kim, Soon-Ok. Production of coenzyme Q10 by recombinant E. coli harboring the decaprenyl diphosphate synthase gene from Sinorhizobium meliloti. Journal of Microbiology and Biotechnology (2006), 16(6), 933-938.

Material Safety Data Sheet (MSDS)

Not Available

General References

Siciliano G, Mancuso M, Tedeschi D, Manca ML, Renna MR, Lombardi V, Rocchi A, Martelli F, Murri L: Coenzyme Q10, exercise lactate and CTG trinucleotide expansion in myotonic dystrophy. Brain Res Bull. 2001 Oct-Nov 1;56(3-4):405-10. [PubMed:11719279 ]
Appelkvist EL, Edlund C, Low P, Schedin S, Kalen A, Dallner G: Effects of inhibitors of hydroxymethylglutaryl coenzyme A reductase on coenzyme Q and dolichol biosynthesis. Clin Investig. 1993;71(8 Suppl):S97-102. [PubMed:8241713 ]
Lalani SR, Vladutiu GD, Plunkett K, Lotze TE, Adesina AM, Scaglia F: Isolated mitochondrial myopathy associated with muscle coenzyme Q10 deficiency. Arch Neurol. 2005 Feb;62(2):317-20. [PubMed:15710863 ]
Mosca L, Marcellini S, Perluigi M, Mastroiacovo P, Moretti S, Famularo G, Peluso I, Santini G, De Simone C: Modulation of apoptosis and improved redox metabolism with the use of a new antioxidant formula. Biochem Pharmacol. 2002 Apr 1;63(7):1305-14. [PubMed:11960607 ]
Zierz S, von Wersebe O, Bleistein J, Jerusalem F: Exogenous coenzyme Q (coq) fails to increase coq in skeletal muscle of two patients with mitochondrial myopathies. J Neurol Sci. 1990 Mar;95(3):283-90. [PubMed:2358821 ]
Sekine K, Ota N, Nishii M, Uetake T, Shimadzu M: Estimation of plasma and saliva levels of coenzyme Q10 and influence of oral supplementation. Biofactors. 2005;25(1-4):205-11. [PubMed:16873948 ]
Zhou S, Zhang Y, Davie A, Marshall-Gradisnik S, Hu H, Wang J, Brushett D: Muscle and plasma coenzyme Q10 concentration, aerobic power and exercise economy of healthy men in response to four weeks of supplementation. J Sports Med Phys Fitness. 2005 Sep;45(3):337-46. [PubMed:16230985 ]
Folkers K, Hanioka T, Xia LJ, McRee JT Jr, Langsjoen P: Coenzyme Q10 increases T4/T8 ratios of lymphocytes in ordinary subjects and relevance to patients having the AIDS related complex. Biochem Biophys Res Commun. 1991 Apr 30;176(2):786-91. [PubMed:1673841 ]
Mancini A, De Marinis L, Oradei A, Hallgass ME, Conte G, Pozza D, Littarru GP: Coenzyme Q10 concentrations in normal and pathological human seminal fluid. J Androl. 1994 Nov-Dec;15(6):591-4. [PubMed:7721661 ]
Hanisch F, Zierz S: Only transient increase of serum CoQ subset 10 during long-term CoQ10 therapy in mitochondrial ophthalmoplegia. Eur J Med Res. 2003 Nov 12;8(11):485-91. [PubMed:14644702 ]
Ogasahara S, Engel AG, Frens D, Mack D: Muscle coenzyme Q deficiency in familial mitochondrial encephalomyopathy. Proc Natl Acad Sci U S A. 1989 Apr;86(7):2379-82. [PubMed:2928337 ]
Ye CQ, Folkers K, Tamagawa H, Pfeiffer C: A modified determination of coenzyme Q10 in human blood and CoQ10 blood levels in diverse patients with allergies. Biofactors. 1988 Dec;1(4):303-6. [PubMed:3255359 ]
Singh RB, Niaz MA, Rastogi SS, Shukla PK, Thakur AS: Effect of hydrosoluble coenzyme Q10 on blood pressures and insulin resistance in hypertensive patients with coronary artery disease. J Hum Hypertens. 1999 Mar;13(3):203-8. [PubMed:10204818 ]
Van Maldergem L, Trijbels F, DiMauro S, Sindelar PJ, Musumeci O, Janssen A, Delberghe X, Martin JJ, Gillerot Y: Coenzyme Q-responsive Leigh's encephalopathy in two sisters. Ann Neurol. 2002 Dec;52(6):750-4. [PubMed:12447928 ]
Tomasetti M, Alleva R, Solenghi MD, Littarru GP: Distribution of antioxidants among blood components and lipoproteins: significance of lipids/CoQ10 ratio as a possible marker of increased risk for atherosclerosis. Biofactors. 1999;9(2-4):231-40. [PubMed:10416035 ]
Ogasahara S, Yorifuji S, Nishikawa Y, Takahashi M, Wada K, Hazama T, Nakamura Y, Hashimoto S, Kono N, Tarui S: Improvement of abnormal pyruvate metabolism and cardiac conduction defect with coenzyme Q10 in Kearns-Sayre syndrome. Neurology. 1985 Mar;35(3):372-7. [PubMed:3974895 ]
Mancini A, Conte B, De Marinis L, Hallgass ME, Pozza D, Oradei A, Littarru GP: Coenzyme Q10 levels in human seminal fluid: diagnostic and clinical implications. Mol Aspects Med. 1994;15 Suppl:s249-55. [PubMed:7752837 ]
Zierz S, Jahns G, Jerusalem F: Coenzyme Q in serum and muscle of 5 patients with Kearns-Sayre syndrome and 12 patients with ophthalmoplegia plus. J Neurol. 1989 Feb;236(2):97-101. [PubMed:2709060 ]
Miyake Y, Shouzu A, Nishikawa M, Yonemoto T, Shimizu H, Omoto S, Hayakawa T, Inada M: Effect of treatment with 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors on serum coenzyme Q10 in diabetic patients. Arzneimittelforschung. 1999 Apr;49(4):324-9. [PubMed:10337451 ]
De Luca C, Filosa A, Grandinetti M, Maggio F, Lamba M, Passi S: Blood antioxidant status and urinary levels of catecholamine metabolites in beta-thalassemia. Free Radic Res. 1999 Jun;30(6):453-62. [PubMed:10400457 ]
Siemieniuk E, Skrzydlewska E: [Coenzyme Q10: its biosynthesis and biological significance in animal organisms and in humans]. Postepy Hig Med Dosw (Online). 2005;59:150-9. [PubMed:15928598 ]
Littarru GP, Tiano L: Bioenergetic and antioxidant properties of coenzyme Q10: recent developments. Mol Biotechnol. 2007 Sep;37(1):31-7. [PubMed:17914161 ]

Only showing the first 10 proteins. There are 17 proteins in total.

Show all enzymes and transporters

Enzymes

Enzyme Details

1. NADH-ubiquinone oxidoreductase chain 1

General function:: Involved in oxidation reduction
Specific function:: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Gene Name:: MT-ND1
Uniprot ID:: P03886
Molecular weight:: 35660.055

Reactions

NADH + Coenzyme Q10 → NAD + QH(2)	details

Enzyme Details

2. NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial

General function:: Involved in oxidoreductase activity, acting on NADH or NADPH
Specific function:: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Gene Name:: NDUFS2
Uniprot ID:: O75306
Molecular weight:: 51851.59

Reactions

NADH + Coenzyme Q10 → NAD + QH(2)	details

Enzyme Details

3. NADH-ubiquinone oxidoreductase chain 4L

General function:: Involved in oxidoreductase activity, acting on NADH or NADPH
Specific function:: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Gene Name:: MT-ND4L
Uniprot ID:: P03901
Molecular weight:: 10741.005

Reactions

NADH + Coenzyme Q10 → NAD + QH(2)	details

Enzyme Details

4. NADH-ubiquinone oxidoreductase chain 5

General function:: Involved in NADH dehydrogenase (ubiquinone) activity
Specific function:: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Gene Name:: MT-ND5
Uniprot ID:: P03915
Molecular weight:: 67025.67

Reactions

NADH + Coenzyme Q10 → NAD + QH(2)	details

Enzyme Details

5. NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial

General function:: Involved in oxidoreductase activity, acting on NADH or NADPH
Specific function:: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Gene Name:: NDUFS3
Uniprot ID:: O75489
Molecular weight:: 30241.245

Reactions

NADH + Coenzyme Q10 → NAD + QH(2)	details

Enzyme Details

6. NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial

General function:: Involved in oxidoreductase activity
Specific function:: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Gene Name:: NDUFV2
Uniprot ID:: P19404
Molecular weight:: 27391.36

Reactions

NADH + Coenzyme Q10 → NAD + QH(2)	details

Enzyme Details

7. Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

General function:: Involved in electron carrier activity
Specific function:: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Can act as a tumor suppressor.
Gene Name:: SDHA
Uniprot ID:: P31040
Molecular weight:: 72690.975

Reactions

Succinic acid + Coenzyme Q10 → Fumaric acid + QH(2)	details

Enzyme Details

8. NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial

General function:: Involved in electron carrier activity
Specific function:: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). May donate electrons to ubiquinone.
Gene Name:: NDUFS8
Uniprot ID:: O00217
Molecular weight:: 23704.795

Reactions

NADH + Coenzyme Q10 → NAD + QH(2)	details

Enzyme Details

9. NADH-ubiquinone oxidoreductase chain 2

General function:: Involved in NADH dehydrogenase (ubiquinone) activity
Specific function:: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Gene Name:: MT-ND2
Uniprot ID:: P03891
Molecular weight:: 38960.47

Reactions

NADH + Coenzyme Q10 → NAD + QH(2)	details

Enzyme Details

10. NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

General function:: Involved in electron carrier activity
Specific function:: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized.
Gene Name:: NDUFS1
Uniprot ID:: P28331
Molecular weight:: 67523.595

Reactions

NADH + Coenzyme Q10 → NAD + QH(2)	details

Only showing the first 10 proteins. There are 17 proteins in total.

Show all enzymes and transporters

Showing metabocard for Coenzyme Q10 (HMDB0001072)

Structure for HMDB0001072 (Coenzyme Q10)

Enzymes

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