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Human Metabolome Database Version 3.5

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Showing metabocard for Dihydrolipoamide (HMDB00985)

Record Information
Version 3.5
Creation Date 2005-11-16 08:48:42 -0700
Update Date 2013-02-08 17:09:42 -0700
HMDB ID HMDB00985
Secondary Accession Numbers
  • HMDB06948
Metabolite Identification
Common Name Dihydrolipoamide
Description Dihydrolipoamide 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
Download: MOL | SDF | SMILES | InChI
Display: 2D Structure | 3D Structure
Synonyms
  1. 6,8-Bis-sulfanyloctanamide
  2. 6,8-Dimercapto-Octanamide
  3. 6,8-Dimercaptooctanamide
  4. 6,8-Disulfanyloctanamide
  5. Dihydrolipoamide
  6. Dihydrothioctamide
Chemical Formula C8H17NOS2
Average Molecular Weight 207.357
Monoisotopic Molecular Weight 207.075155551
IUPAC Name 6,8-disulfanyloctanimidic acid
Traditional IUPAC Name 6,8-disulfanyloctanimidic acid
CAS Registry Number 3884-47-7
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 Key VLYUGYAKYZETRF-UHFFFAOYSA-N
Chemical Taxonomy
Kingdom Organic Compounds
Super Class Aliphatic Acyclic Compounds
Class Thiols
Sub Class Alkylthiols
Other Descriptors
  • Thiols
  • a small molecule(Cyc)
  • dithiol(ChEBI)
  • monocarboxylic acid amide(ChEBI)
Substituents
  • Imine
Direct Parent Alkylthiols
Ontology
Status Expected and Not Quantified
Origin
  • Endogenous
Biofunction Not Available
Application Not Available
Cellular locations
  • Mitochondria
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 0.099 g/L ALOGPS
LogP 2.22 ALOGPS
LogP 1.44 ChemAxon
LogS -3.32 ALOGPS
pKa (strongest acidic) 6.68 ChemAxon
pKa (strongest basic) 8.78 ChemAxon
Hydrogen Acceptor Count 2 ChemAxon
Hydrogen Donor Count 4 ChemAxon
Polar Surface Area 44.08 A2 ChemAxon
Rotatable Bond Count 7 ChemAxon
Refractivity 68.7 ChemAxon
Polarizability 23.77 ChemAxon
Formal Charge 0 ChemAxon
Physiological Charge 0 ChemAxon
Spectra
Not Available
Biological Properties
Cellular Locations
  • Mitochondria
Biofluid Locations Not Available
Tissue Location Not Available
Pathways
Name SMPDB Link KEGG Link
Valine, Leucine and Isoleucine Degradation SMP00032 map00280 Link_out
Normal Concentrations
Not Available
Abnormal Concentrations
Not Available
Associated Disorders and Diseases
Disease References None
Associated OMIM IDs None
DrugBank ID Not Available
Phenol Explorer Compound ID Not Available
Phenol Explorer Metabolite ID Not Available
FoodDB ID FDB022352
KNApSAcK ID Not Available
Chemspider ID 643 Link_out
KEGG Compound ID C00579 Link_out
BioCyc ID DIHYDROLIPOAMIDE Link_out
BiGG ID 35406 Link_out
Wikipedia Link Dihydrolipoamide Link_out
NuGOwiki Link HMDB00985 Link_out
Metagene Link HMDB00985 Link_out
METLIN ID 5920 Link_out
PubChem Compound 663 Link_out
PDB ID Not Available
ChEBI ID 17694 Link_out
References
Synthesis Reference Weitzman, 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 Link_out
  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 Link_out
  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 Link_out
  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 Link_out
  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 Link_out
Enzymes
Name: Dihydrolipoyl dehydrogenase, mitochondrial
Reactions:
  • protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+ [RN:R08550]
Gene Name: DLD
Uniprot ID: P09622 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
Name: Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
Reactions:
  • succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine [RN:R02570]
Gene Name: DLST
Uniprot ID: P36957 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
Name: Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
Reactions:
  • 2-methylpropanoyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-[2-methylpropanoyl]dihydrolipoyl)lysine [RN:R02662]
Gene Name: DBT
Uniprot ID: P11182 Link_out
Protein Sequence: FASTA
Gene Sequence: FASTA
Name: Dihydrolipoamide S-acetyltransferase
Reactions:
    Gene Name: DLAT
    Uniprot ID: Q86YI5 Link_out
    Protein Sequence: FASTA
    Gene Sequence: FASTA