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Record Information
Version3.6
Creation Date2005-11-16 15:48:42 UTC
Update Date2013-02-09 00:09:42 UTC
HMDB IDHMDB00985
Secondary Accession Numbers
  • 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
Thumb
Synonyms
  1. 6,8-Bis-sulfanyloctanamide
  2. 6,8-Dimercapto-Octanamide
  3. 6,8-Dimercaptooctanamide
  4. 6,8-Disulfanyloctanamide
  5. Dihydrolipoamide
  6. Dihydrothioctamide
Chemical FormulaC8H17NOS2
Average Molecular Weight207.357
Monoisotopic Molecular Weight207.075155551
IUPAC Name6,8-disulfanyloctanimidic acid
Traditional IUPAC Name6,8-disulfanyloctanimidic acid
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
KingdomOrganic Compounds
Super ClassAliphatic Acyclic Compounds
ClassThiols
Sub ClassAlkylthiols
Other Descriptors
  • Thiols
  • a small molecule(Cyc)
  • dithiol(ChEBI)
  • monocarboxylic acid amide(ChEBI)
Substituents
  • Imine
Direct ParentAlkylthiols
Ontology
StatusExpected and Not Quantified
Origin
  • Endogenous
BiofunctionNot Available
ApplicationNot Available
Cellular locations
  • Mitochondria
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 Area44.08ChemAxon
Rotatable Bond Count7ChemAxon
Refractivity68.7ChemAxon
Polarizability23.77ChemAxon
Spectra
SpectraNot Available
Biological Properties
Cellular Locations
  • Mitochondria
Biofluid LocationsNot Available
Tissue LocationNot Available
Pathways
NameSMPDB LinkKEGG Link
Valine, Leucine and Isoleucine DegradationSMP00032map00280
Normal Concentrations
Not Available
Abnormal Concentrations
Not Available
Associated Disorders and Diseases
Disease ReferencesNone
Associated OMIM IDsNone
DrugBank IDNot Available
DrugBank Metabolite IDNot Available
Phenol Explorer Compound IDNot Available
Phenol Explorer Metabolite IDNot Available
FoodDB IDFDB022352
KNApSAcK IDNot Available
Chemspider ID643
KEGG Compound IDC00579
BioCyc IDDIHYDROLIPOAMIDE
BiGG ID35406
Wikipedia LinkDihydrolipoamide
NuGOwiki LinkHMDB00985
Metagene LinkHMDB00985
METLIN ID5920
PubChem Compound663
PDB IDNot Available
ChEBI ID17694
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

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
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
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
General function:
Involved in acyltransferase activity
Specific function:
Not Available
Gene Name:
DLAT
Uniprot ID:
Q86YI5
Molecular weight:
68996.0