You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Human Metabolome Database.

Showing metabocard for Dihydrolipoamide (HMDB0000985)

Jump To Section:
IdentificationTaxonomyOntologyPhysical propertiesSpectraBiological propertiesConcentrationsLinksReferencesenzymes (4) Show 4 proteinsXML
enzymes (4) Show 4 proteins
Record Information
Version4.0
StatusExpected but not Quantified
Creation Date2005-11-16 15:48:42 UTC
Update Date2020-02-26 21:22:49 UTC
HMDB IDHMDB0000985
Secondary Accession Numbers
  • HMDB0006948
  • HMDB00985
  • HMDB06948
Metabolite Identification
Common NameDihydrolipoamide
DescriptionDihydrolipoamide is an intermediate in glycolysis/gluconeogenesis, citrate cycle (TCA cycle), alanine, aspartate and pyruvate metabolism, and valine, leucine and isoleucine degradation (KEGG ID C00579). It is converted to lipoamide via the enzyme dihydrolipoamide dehydrogenase [EC:1.8.1.4]. Dihydrolipoamide is also a substrate of enzyme Acyltransferases [EC 2.3.1.-]. (KEGG).
Structure
Data?1582752169
MOLSDFPDBSMILESInChI
Synonyms
ValueSource
6,8-DimercaptooctanamideChEBI
DihydrothioctamideChEBI
6,8-Bis-sulfanyloctanamideHMDB
6,8-Dimercapto-octanamideHMDB
6,8-DisulfanyloctanamideHMDB
Dihydrolipoamide, (+-)-isomerHMDB
Chemical FormulaC8H17NOS2
Average Molecular Weight207.357
Monoisotopic Molecular Weight207.075155551
IUPAC Name6,8-disulfanyloctanimidic acid
Traditional Namedihydrothioctamide
CAS Registry Number3884-47-7
SMILES
OC(=N)CCCCC(S)CCS
InChI Identifier
InChI=1S/C8H17NOS2/c9-8(10)4-2-1-3-7(12)5-6-11/h7,11-12H,1-6H2,(H2,9,10)
InChI KeyVLYUGYAKYZETRF-UHFFFAOYSA-N
Chemical Taxonomy
Description belongs to the class of organic compounds known as fatty amides. These are carboxylic acid amide derivatives of fatty acids, that are formed from a fatty acid and an amine.
KingdomOrganic compounds
Super ClassLipids and lipid-like molecules
ClassFatty Acyls
Sub ClassFatty amides
Direct ParentFatty amides
Alternative Parents
Substituents
  • Fatty amide
  • Primary carboxylic acid amide
  • Carboxamide group
  • Carboxylic acid derivative
  • Alkylthiol
  • Organic nitrogen compound
  • Organic oxygen compound
  • Organopnictogen compound
  • Organic oxide
  • Hydrocarbon derivative
  • Organosulfur compound
  • Organooxygen compound
  • Organonitrogen compound
  • Carbonyl group
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External Descriptors
Ontology
Disposition

Route of exposure:

Source:

Biological location:

Process

Naturally occurring process:

Role

Biological role:

Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting PointNot AvailableNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Properties
PropertyValueSource
Water Solubility0.099 g/LALOGPS
logP2.22ALOGPS
logP1.44ChemAxon
logS-3.3ALOGPS
pKa (Strongest Acidic)6.68ChemAxon
pKa (Strongest Basic)8.78ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count2ChemAxon
Hydrogen Donor Count4ChemAxon
Polar Surface Area44.08 ŲChemAxon
Rotatable Bond Count7ChemAxon
Refractivity68.7 m³·mol⁻¹ChemAxon
Polarizability23.77 ųChemAxon
Number of Rings0ChemAxon
BioavailabilityYesChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleNoChemAxon
MDDR-like RuleNoChemAxon
Spectra
Spectrum TypeDescriptionSplash KeyView
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (Non-derivatized) - 70eV, Positivesplash10-0006-9700000000-936a7170a2da09aecf11Spectrum
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (1 TMS) - 70eV, Positivesplash10-00di-9410000000-9f1410bc40e59db39d21Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-0ab9-1960000000-1e45a79f64407fb4dea8Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-0ab9-5930000000-297b157da8ed63567faaSpectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-0006-9000000000-82e7dacb48c8cab103d4Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-0a4l-0940000000-f34746a5ea022152ba75Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-052f-1900000000-99beaa28d55837788743Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0m2i-9400000000-53152f2f29c03cd0cbcdSpectrum
Biological Properties
Cellular Locations
  • Mitochondria
Biospecimen LocationsNot Available
Tissue LocationsNot Available
Pathways
Normal Concentrations
Not Available
Abnormal Concentrations
Not Available
Associated Disorders and Diseases
Disease ReferencesNone
Associated OMIM IDsNone
DrugBank IDNot Available
Phenol Explorer Compound IDNot Available
FooDB IDFDB022352
KNApSAcK IDNot Available
Chemspider ID643
KEGG Compound IDC00579
BioCyc IDNot Available
BiGG ID35406
Wikipedia LinkDihydrolipoamide
METLIN ID5920
PubChem Compound663
PDB IDNot Available
ChEBI ID17694
Food Biomarker OntologyNot Available
VMH IDNot Available
MarkerDB ID
References
Synthesis ReferenceWeitzman, P. D. J.; Hewson, Janet K.; Parker, M. G. Preparation of dihydrolipoamide by electrolytic reduction. FEBS Letters (1974), 43(1), 101-3.
Material Safety Data Sheet (MSDS)Not Available
General References
  1. Brautigam CA, Chuang JL, Tomchick DR, Machius M, Chuang DT: Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations. J Mol Biol. 2005 Jul 15;350(3):543-52. [PubMed:15946682 ]
  2. Kim H: Asparagine-473 residue is important to the efficient function of human dihydrolipoamide dehydrogenase. J Biochem Mol Biol. 2005 Mar 31;38(2):248-52. [PubMed:15826505 ]
  3. McMillan PJ, Stimmler LM, Foth BJ, McFadden GI, Muller S: The human malaria parasite Plasmodium falciparum possesses two distinct dihydrolipoamide dehydrogenases. Mol Microbiol. 2005 Jan;55(1):27-38. [PubMed:15612914 ]
  4. Li XJ, Grunwald D, Mathieu J, Morel F, Stasia MJ: Crucial role of two potential cytosolic regions of Nox2, 191TSSTKTIRRS200 and 484DESQANHFAVHHDEEKD500, on NADPH oxidase activation. J Biol Chem. 2005 Apr 15;280(15):14962-73. Epub 2005 Jan 31. [PubMed:15684431 ]
  5. Deres P, Halmosi R, Toth A, Kovacs K, Palfi A, Habon T, Czopf L, Kalai T, Hideg K, Sumegi B, Toth K: Prevention of doxorubicin-induced acute cardiotoxicity by an experimental antioxidant compound. J Cardiovasc Pharmacol. 2005 Jan;45(1):36-43. [PubMed:15613977 ]

Enzymes

Enzyme Details
1. Dihydrolipoyl dehydrogenase, mitochondrial
General function:
Involved in oxidoreductase activity
Specific function:
Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction.
Gene Name:
DLD
Uniprot ID:
P09622
Molecular weight:
54176.91
Reactions
Dihydrolipoamide + NAD → Lipoamide + NADH + Hydrogen Iondetails
Enzyme Details
2. Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
General function:
Involved in acyltransferase activity
Specific function:
The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
Gene Name:
DLST
Uniprot ID:
P36957
Molecular weight:
48754.87
Enzyme Details
3. Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
General function:
Involved in acyltransferase activity
Specific function:
The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
Gene Name:
DBT
Uniprot ID:
P11182
Molecular weight:
53486.635
Enzyme Details
4. Dihydrolipoamide S-acetyltransferase
General function:
Involved in acyltransferase activity
Specific function:
Not Available
Gene Name:
DLAT
Uniprot ID:
Q86YI5
Molecular weight:
68996.0