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Record Information
StatusDetected and Quantified
Creation Date2006-08-13 15:11:32 UTC
Update Date2020-02-26 21:25:04 UTC
Secondary Accession Numbers
  • HMDB04246
Metabolite Identification
Common NameBradykinin
DescriptionBradykinin is a vasoactive kinin that is liberated from its substrate kininogen by the action of kallikrein, and is known to be involved in a wide range of biologic processes. It may play an important role in blood pressure regulation and the maintenance of normal blood flow. Moreover, in various pathologic states of the cardiovascular system, it appears to provide protective actions against ischemic injury, ventricular hypertrophy, congestive heart failure, and thrombosis. Bradykinin is a potent vasodilator that acts through endothelial B2 kinin receptors to stimulate the release of nitric oxide and endothelium-derived hyperpolarizing factor. Bradykinin deficiency states may play a role in some forms of hypertension, and a relative deficiency in bradykinin may be a contributing factor to worsening heart failure. Experimental studies revealed that mice lacking the B2 receptor gene were more likely to develop hypertension, cardiac hypertrophy, and myocardial damage. Kinins exert several biologic actions. They are involved in nociception, inflammation, capillary permeability, reactive hyperemia, and stimulation of cellular glucose uptake. Bradykinin is a polypeptide that circulates in the plasma in very low concentrations in comparison with the amount of bradykinin found in various body tissues. Kininogens ([alpha] 2 globulins) are synthesized in the liver and circulate at high concentrations in the plasma. There are two kininogenases that convert kininogens into bradykinin: plasma kallikrein, also known as Fletcher factor, and glandular kallikrein, also known as tissue kallikrein. (PMID: 11975815 ).
Callidin IHMDB
Kallidin 9HMDB
Kallidin IHMDB
Bradykinin acetate, (9-D-arg)-isomerHMDB
Bradykinin hydrochlorideHMDB
Bradykinin triacetateHMDB
Bradykinin, (2-D-pro-7-D-pro)-isomerHMDB
Bradykinin, (8-D-phe)-isomerHMDB
Arg pro pro gly phe ser pro phe argHMDB
Bradykinin, (1-D-arg)-isomerHMDB
Bradykinin, (2-D-pro-3-D-pro-7-D-pro)-isomerHMDB
Bradykinin, (3-D-pro-7-D-pro)-isomerHMDB
Bradykinin, (5-D-phe)-isomerHMDB
Bradykinin, (5-D-phe-8-D-phe)-isomerHMDB
Bradykinin, (6-D-ser)-isomerHMDB
Bradykinin, (7-D-pro)-isomerHMDB
Bradykinin, (9-D-arg)-isomerHMDB
Bradykinin diacetateHMDB
Bradykinin, (2-D-pro)-isomerHMDB
Bradykinin, (3-D-pro)-isomerHMDB
Chemical FormulaC50H73N15O11
Average Molecular Weight1060.2085
Monoisotopic Molecular Weight1059.561398253
IUPAC Name(2S)-2-[(2S)-2-{[(2S)-1-[(2S)-2-[(2S)-2-(2-{[(2S)-1-[(2S)-1-[(2S)-2-amino-5-carbamimidamidopentanoyl]pyrrolidine-2-carbonyl]pyrrolidin-2-yl]formamido}acetamido)-3-phenylpropanamido]-3-hydroxypropanoyl]pyrrolidin-2-yl]formamido}-3-phenylpropanamido]-5-carbamimidamidopentanoic acid
Traditional NameL-bradykinin
CAS Registry Number58-82-2
InChI Identifier
Chemical Taxonomy
Description belongs to the class of organic compounds known as oligopeptides. These are organic compounds containing a sequence of between three and ten alpha-amino acids joined by peptide bonds.
KingdomOrganic compounds
Super ClassOrganic acids and derivatives
ClassCarboxylic acids and derivatives
Sub ClassAmino acids, peptides, and analogues
Direct ParentOligopeptides
Alternative Parents
  • Alpha-oligopeptide
  • Phenylalanine or derivatives
  • Proline or derivatives
  • N-acyl-alpha amino acid or derivatives
  • N-acyl-l-alpha-amino acid
  • N-acyl-alpha-amino acid
  • Alpha-amino acid amide
  • N-substituted-alpha-amino acid
  • Alpha-amino acid or derivatives
  • Amphetamine or derivatives
  • N-acylpyrrolidine
  • Pyrrolidine carboxylic acid or derivatives
  • Pyrrolidine-2-carboxamide
  • Monocyclic benzene moiety
  • Fatty acyl
  • Benzenoid
  • Fatty amide
  • Tertiary carboxylic acid amide
  • Pyrrolidine
  • Secondary carboxylic acid amide
  • Carboxamide group
  • Amino acid or derivatives
  • Guanidine
  • Amino acid
  • Azacycle
  • Organoheterocyclic compound
  • Carboxylic acid
  • Organic 1,3-dipolar compound
  • Propargyl-type 1,3-dipolar organic compound
  • Monocarboxylic acid or derivatives
  • Carboximidamide
  • Amine
  • Organopnictogen compound
  • Organic oxygen compound
  • Organic nitrogen compound
  • Carbonyl group
  • Alcohol
  • Primary aliphatic amine
  • Organic oxide
  • Hydrocarbon derivative
  • Primary amine
  • Primary alcohol
  • Organonitrogen compound
  • Organooxygen compound
  • Aromatic heteromonocyclic compound
Molecular FrameworkAromatic heteromonocyclic compounds
External Descriptors


Biological location:


Naturally occurring process:


Industrial application:

Physical Properties
Experimental Properties
Melting PointNot AvailableNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Properties
Water Solubility0.057 g/LALOGPS
pKa (Strongest Acidic)3.39ChemAxon
pKa (Strongest Basic)12.44ChemAxon
Physiological Charge2ChemAxon
Hydrogen Acceptor Count18ChemAxon
Hydrogen Donor Count14ChemAxon
Polar Surface Area413.78 ŲChemAxon
Rotatable Bond Count27ChemAxon
Refractivity295.08 m³·mol⁻¹ChemAxon
Polarizability109.98 ųChemAxon
Number of Rings5ChemAxon
Rule of FiveNoChemAxon
Ghose FilterNoChemAxon
Veber's RuleNoChemAxon
MDDR-like RuleYesChemAxon
Spectrum TypeDescriptionSplash KeyView
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-00di-9605021310-963d37a5c0a6a8c3b581Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-00fr-4914021100-da28e55acbc5e55e7615Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-00di-9824010200-b5b2c55602c29375ed1aSpectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-0ard-9000000008-70e85b5126294f4866f8Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-0a4m-8001001009-d8431ee82b28629bac33Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-0a4i-9001111000-9de36ae5c0196bc1ca98Spectrum
Biological Properties
Cellular LocationsNot Available
Biospecimen Locations
  • Prostate Tissue
Tissue Locations
  • Prostate
Normal Concentrations
Not Available
Abnormal Concentrations
Prostate TissueDetected and Quantified0.5 (0.0-1.0) umol/g tissueAdult (>18 years old)Both
Prostate cancer
Associated Disorders and Diseases
Disease References
Prostate cancer
  1. Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4. doi: 10.1038/nature07762. [PubMed:19212411 ]
Associated OMIM IDs
DrugBank IDDB12126
Phenol Explorer Compound IDNot Available
FooDB IDFDB023350
KNApSAcK IDNot Available
Chemspider ID388341
KEGG Compound IDC00306
BioCyc IDNot Available
BiGG IDNot Available
Wikipedia LinkBradykinin
METLIN IDNot Available
PubChem Compound439201
PDB IDNot Available
ChEBI ID3165
Food Biomarker OntologyNot Available
VMH IDNot Available
Synthesis ReferencePostnov, V. N. Some aspects of the synthesis of organic functional groups on inorganic matrices. Napravl. Sintez Tverd. Veshchestv (1987), (2), 109-20.
Material Safety Data Sheet (MSDS)Download (PDF)
General References
  1. Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4. doi: 10.1038/nature07762. [PubMed:19212411 ]
  2. Palkhiwala SA, Frishman WH, Warshafsky S: Bradykinin for the treatment of cardiovascular disease. Heart Dis. 2001 Sep-Oct;3(5):333-9. [PubMed:11975815 ]

Only showing the first 10 proteins. There are 15 proteins in total.


General function:
Involved in metallopeptidase activity
Specific function:
Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in serine-type endopeptidase activity
Specific function:
Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta- factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in cysteine-type endopeptidase inhibitor activity
Specific function:
(1) Kininogens are inhibitors of thiol proteases; (2) HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; (3) HMW-kininogen inhibits the thrombin- and plasmin- induced aggregation of thrombocytes; (4) the active peptide bradykinin that is released from HMW-kininogen shows a variety of physiological effects:(4A) influence in smooth muscle contraction, (4B) induction of hypotension, (4C) natriuresis and diuresis, (4D) decrease in blood glucose level, (4E) it is a mediator of inflammation and causes (4E1) increase in vascular permeability, (4E2) stimulation of nociceptors (4E3) release of other mediators of inflammation (e.g. prostaglandins), (4F) it has a cardioprotective effect (directly via bradykinin action, indirectly via endothelium-derived relaxing factor action); (5) LMW-kininogen inhibits the aggregation of thrombocytes; (6) LMW- kininogen is in contrast to HMW-kininogen not involved in blood clotting
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in serine-type endopeptidase activity
Specific function:
The enzyme cleaves Lys-Arg and Arg-Ser bonds. It activates, in a reciprocal reaction, factor XII after its binding to a negatively charged surface. It also releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in G-protein coupled receptor protein signaling pathway
Specific function:
Receptor for angiotensin II. Mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in G-protein coupled receptor protein signaling pathway
Specific function:
Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Not Available
Specific function:
Play a role as NO/PRKG1-dependent regulator of IP3- induced calcium release; its phosphorylation by PRKG1 inhibits bradykinin and IP3-induced calcium release from intracellular stores. Recruits PRKG1 to the endoplasmic reticulum and may mediate the assembly of PRKG1 and ITPR1 in a macrocomplex. Involved in PRKG1 signaling cascade leading to inhibition of platelet activation and aggregation. Mediates also NO-dependent inhibition of calcium signaling in gastrointestinal smooth muscle contributing to NO-dependent relaxation
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in G-protein coupled receptor protein signaling pathway
Specific function:
High affinity receptor for INSL5. Also acts as receptor for RLN3/relaxin-3, as well as bradykinin and kallidin. Binding of the ligand inhibit cAMP accumulation
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in proteolysis
Specific function:
Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I- binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney
Gene Name:
Uniprot ID:
Molecular weight:
General function:
Involved in metalloendopeptidase activity
Specific function:
Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A
Gene Name:
Uniprot ID:
Molecular weight:

Only showing the first 10 proteins. There are 15 proteins in total.