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| Name | Formic Acid | |||||||||||||||||||||||||||||||||||||||
| Accession Number | DB01942 (EXPT01461) | |||||||||||||||||||||||||||||||||||||||
| Type | small molecule | |||||||||||||||||||||||||||||||||||||||
| Groups | experimental | |||||||||||||||||||||||||||||||||||||||
| Description | Formic acid (systematically called methanoic acid) is the simplest carboxylic acid. It is an important intermediate in chemical synthesis and occurs naturally, most famously in the venom of bee and ant stings. The principal use of formic acid is as a preservative and antibacterial agent in livestock feed. [Wikipedia] |
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| Structure |
Download: MOL | SDF | SMILES | InChI Display: 2D Structure | 3D Structure |
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| Synonyms |
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| Salts | Not Available | |||||||||||||||||||||||||||||||||||||||
| Brand names | Not Available | |||||||||||||||||||||||||||||||||||||||
| Brand mixtures | Not Available | |||||||||||||||||||||||||||||||||||||||
| Categories |
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| CAS number | 64-18-6 | |||||||||||||||||||||||||||||||||||||||
| Weight |
Average: 46.0254 Monoisotopic: 46.005479308 |
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| Chemical Formula | CH2O2 | |||||||||||||||||||||||||||||||||||||||
| InChI Key | InChIKey=BDAGIHXWWSANSR-UHFFFAOYSA-N | |||||||||||||||||||||||||||||||||||||||
| InChI |
InChI=1S/CH2O2/c2-1-3/h1H,(H,2,3)
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| IUPAC Name |
formic acid
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| SMILES |
OC=O
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| Mass Spec | show (7.52 KB) | |||||||||||||||||||||||||||||||||||||||
| Taxonomy | ||||||||||||||||||||||||||||||||||||||||
| Kingdom | Not Available | |||||||||||||||||||||||||||||||||||||||
| Classes | Not Available | |||||||||||||||||||||||||||||||||||||||
| Substructures | Not Available | |||||||||||||||||||||||||||||||||||||||
| Pharmacology | ||||||||||||||||||||||||||||||||||||||||
| Indication | Not Available | |||||||||||||||||||||||||||||||||||||||
| Pharmacodynamics | Not Available | |||||||||||||||||||||||||||||||||||||||
| Mechanism of action | Not Available | |||||||||||||||||||||||||||||||||||||||
| Absorption | Formic acid is readily metabolized and eliminated by the body. | |||||||||||||||||||||||||||||||||||||||
| Volume of distribution | Not Available | |||||||||||||||||||||||||||||||||||||||
| Protein binding | Not Available | |||||||||||||||||||||||||||||||||||||||
| Metabolism |
Not Available
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| Route of elimination | Not Available | |||||||||||||||||||||||||||||||||||||||
| Half life | Not Available | |||||||||||||||||||||||||||||||||||||||
| Clearance | Not Available | |||||||||||||||||||||||||||||||||||||||
| Toxicity | ORAL (LD50): Acute: 700 mg/kg [Mouse]. 1100 mg/kg [Rat]. 4000 mg/kg [Dog]. | |||||||||||||||||||||||||||||||||||||||
| Affected organisms | Not Available | |||||||||||||||||||||||||||||||||||||||
| Pathways | Not Available | |||||||||||||||||||||||||||||||||||||||
| Pharmacoeconomics | ||||||||||||||||||||||||||||||||||||||||
| Manufacturers | Not Available | |||||||||||||||||||||||||||||||||||||||
| Packagers | Not Available | |||||||||||||||||||||||||||||||||||||||
| Dosage forms | Not Available | |||||||||||||||||||||||||||||||||||||||
| Prices | Not Available | |||||||||||||||||||||||||||||||||||||||
| Patents | Not Available | |||||||||||||||||||||||||||||||||||||||
| Properties | ||||||||||||||||||||||||||||||||||||||||
| State | liquid | |||||||||||||||||||||||||||||||||||||||
| Experimental Properties |
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| Predicted Properties |
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| Synthesis Reference | Not Available | |||||||||||||||||||||||||||||||||||||||
| General Reference | Not Available | |||||||||||||||||||||||||||||||||||||||
| External Links |
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| ATC Codes | Not Available | |||||||||||||||||||||||||||||||||||||||
| AHFS Codes | Not Available | |||||||||||||||||||||||||||||||||||||||
| PDB Entries | ||||||||||||||||||||||||||||||||||||||||
| FDA label | Not Available | |||||||||||||||||||||||||||||||||||||||
| MSDS | show (78.4 KB) | |||||||||||||||||||||||||||||||||||||||
| Interactions | ||||||||||||||||||||||||||||||||||||||||
| Drug Interactions | Not Available | |||||||||||||||||||||||||||||||||||||||
| Food Interactions | Not Available | |||||||||||||||||||||||||||||||||||||||
| Targets |
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Pharmacological action: unknown
Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed Organism class: humanUniProt ID: P09601 ![]() Gene: HMOX1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA Organism class: humanUniProt ID: P07998 ![]() Gene: RNASE1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
3. Dihydroorotate dehydrogenase Pharmacological action: unknown(S)-dihydroorotate + O(2) = orotate + H(2)O(2) Organism class: bacterialUniProt ID: P0A7E1 ![]() Gene: pyrD Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 4. (S)-2-haloacid dehalogenase Pharmacological action: unknownCatalyzes the hydrolytic dehalogenation of small L-2- haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Active with 2-halogenated carboxylic acids and converts only the L-isomer of 2-chloropropionic acid with inversion of configuration to produce D-lactate Organism class: bacterialUniProt ID: Q60099 ![]() Gene: dhlB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
This is an oxacillin-hydrolyzing beta-lactamase Organism class: bacterialUniProt ID: P0A1V8 ![]() Gene: bla Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 6. Catalase Pharmacological action: unknownDecomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide Organism class: bacterialUniProt ID: P42321 ![]() Gene: katA Protein Sequence: FASTA SNPs: SNPJam Report ![]() References: 7. Signal recognition particle protein Pharmacological action: unknownNecessary for efficient export of extracytoplasmic proteins. Binds to the signal sequence when it emerges from the ribosomes Organism class: bacterialUniProt ID: O07347 ![]() Gene: ffh Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 8. Streptavidin Pharmacological action: unknownThe biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin) Organism class: bacterialUniProt ID: P22629 ![]() Protein Sequence: FASTA Gene Sequence: FASTA References:
Pharmacological action: unknown
Glycerone phosphate = methylglyoxal + phosphate Organism class: bacterialUniProt ID: P0A733 ![]() Gene: mgsA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 10. C-terminal-binding protein 1 Pharmacological action: unknownInvolved in controlling the equilibrium between tubular and stacked structures in the Golgi complex (By similarity). Co- repressor targeting diverse transcription regulators such as GLIS2. Has dehydrogenase activity Organism class: humanUniProt ID: Q13363 ![]() Gene: CTBP1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Hydrolysis of 6-phosphogluconolactone to 6- phosphogluconate Organism class: bacterialUniProt ID: Q9X0N8 ![]() Gene: pgl Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 12. Citrate lyase beta subunit-like protein Pharmacological action: unknownMay play a role in fatty acid biosynthesis (Potential) Organism class: bacterialUniProt ID: O06162 ![]() Gene: citE Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 13. Peripheral plasma membrane protein CASK Pharmacological action: unknownMultidomain scaffolding protein with a role in synaptic transmembrane protein anchoring and ion channel trafficking. Contributes to neural development and regulation of gene expression via interaction with the transcription factor TRB1. Binds to cell-surface proteins, including amyloid precursor protein, neurexins and syndecans. May mediate a link between the extracellular matrix and the actin cytoskeleton via its interaction with syndecan and with the actin/spectrin-binding protein 4.1 Organism class: humanUniProt ID: O14936 ![]() Gene: CASK Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 14. Guanylate kinase Pharmacological action: unknownEssential for recycling GMP and indirectly, cGMP (By similarity) Organism class: bacterialUniProt ID: P0A5I4 ![]() Gene: gmk Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 15. Probable butyrate kinase 2 Pharmacological action: unknownATP + butanoate = ADP + butanoyl phosphate Organism class: bacterialUniProt ID: Q9X278 ![]() Gene: buk2 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 16. AIG2-like domain-containing protein 1 Pharmacological action: unknownOrganism class: human UniProt ID: Q9BVM4 ![]() Gene: A2LD1 SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: human UniProt ID: P20472 ![]() Gene: PVALB SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: human UniProt ID: P14621 ![]() Gene: ACYP2 SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: bacterial UniProt ID: Q81C15 ![]() Gene: BC_2969 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 20. Arginine N-succinyltransferase subunit alpha Pharmacological action: unknownCatalyzes the transfer of succinyl-CoA to arginine to produce 2-N-succinylarginine. Also acts on L-ornithine Organism class: bacterialUniProt ID: P80357 ![]() Gene: astA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 21. Mannose-6-phosphate isomerase Pharmacological action: unknownD-mannose 6-phosphate = D-fructose 6- phosphate Organism class: bacterialUniProt ID: P39841 ![]() Gene: yvyI Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 22. Nitric-oxide synthase, brain Pharmacological action: unknownProduces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter Organism class: humanUniProt ID: P29475 ![]() Gene: NOS1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
23. Oligopeptide ABC transporter, periplasmic oligopeptide-binding protein Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9X0V0 ![]() Gene: TM_1223 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Organism class: bacterial UniProt ID: P75914 ![]() Gene: ycdX Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 25. Phenazine biosynthesis protein PhzD Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q7DC80 ![]() Gene: phzD1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 26. Oxalate decarboxylase oxdC Pharmacological action: unknownConverts oxalate to formate and CO(2) in an O(2)- dependent reaction. Can also catalyze minor side reactions:oxalate oxidation to produce H(2)O(2), and oxalate-dependent, H(2)O(2)-independent dye oxidations Organism class: bacterialUniProt ID: O34714 ![]() Gene: oxdC Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 27. Putative ketoacyl reductase Pharmacological action: unknownOrganism class: bacterial UniProt ID: P16544 ![]() Gene: actIII Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 28. Gephyrin Pharmacological action: unknownMicrotubule-associated protein involved in membrane protein-cytoskeleton interactions. It is thought to anchor the inhibitory glycine receptor (GLYR) to subsynaptic microtubules (By similarity). Involved in molybdenum cofactor biosynthesis. Required for molybdenum transfer to molybdopterin. In a first step, copper-molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released (By similarity) Organism class: humanUniProt ID: Q9NQX3 ![]() Gene: GPHN Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Organism class: bacterial UniProt ID: Q81F54 ![]() Gene: BC_1747 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 30. Cytohesin-2 Pharmacological action: unknownPromotes guanine-nucleotide exchange on ARF1, ARF3 and ARF6. Promotes the activation of ARF through replacement of GDP with GTP Organism class: humanUniProt ID: Q99418 ![]() Gene: CYTH2 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 31. Glutaconyl-CoA decarboxylase subunit alpha Pharmacological action: unknownDecarboxylase subunit of the primary sodium pump glutaconyl-CoA decarboxylase (GCD) Organism class: bacterialUniProt ID: Q06700 ![]() Gene: gcdA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 32. Transcriptional regulator, IclR family Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9WXS0 ![]() Gene: TM_0065 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 33. Hypothetical protein VC1899 Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9KQU9 ![]() Gene: VC_1899 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 34. Catalase Pharmacological action: unknownDecomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide Organism class: bacterialUniProt ID: P77872 ![]() Gene: katA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Organism class: bacterial UniProt ID: Q9X0F9 ![]() Gene: TM_1070 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May also function as a storage protein or ligandin for parasitotoxic ferriprotoporphyrin IX (hemin) Organism class: parasiticUniProt ID: Q8MU52 ![]() Gene: GST Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 37. Hypoxanthine-guanine phosphoribosyltransferase, putative Pharmacological action: unknownGMP + diphosphate = guanine + 5-phospho-alpha- D-ribose 1-diphosphate Organism class: parasiticUniProt ID: Q27796 ![]() Gene: HGPRTase Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 38. Glutaminase 1 Pharmacological action: unknownL-glutamine + H(2)O = L-glutamate + NH(3) Organism class: bacterialUniProt ID: O31465 ![]() Gene: glsA1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 39. Glutaminase 1 Pharmacological action: unknownL-glutamine + H(2)O = L-glutamate + NH(3) Organism class: bacterialUniProt ID: P77454 ![]() Gene: glsA1 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 40. Molybdopterin-converting factor subunit 2 Pharmacological action: unknownConverts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group Organism class: bacterialUniProt ID: P30749 ![]() Gene: moaE Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 41. Aminotransferase, putative Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q9X0L5 ![]() Gene: TM_1131 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]()
Pharmacological action: unknown
Organism class: bacterial UniProt ID: Q9Z4N6 ![]() Gene: fbpA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 43. Gyrase B Pharmacological action: unknownDNA gyrase negatively supercoils closed circular double- stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings (By similarity) Organism class: bacterialUniProt ID: Q9LCX5 ![]() Gene: gyrB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() 44. Protein ygbM Pharmacological action: unknownOrganism class: bacterial UniProt ID: Q46891 ![]() Gene: ygbM Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 45. Delta-aminolevulinic acid dehydratase Pharmacological action: unknown2 5-aminolevulinate = porphobilinogen + 2 H(2)O Organism class: bacterialUniProt ID: Q59643 ![]() Gene: hemB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 46. 3-phosphoshikimate 1-carboxyvinyltransferase Pharmacological action: unknownPhosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate Organism class: bacterialUniProt ID: P0A6D3 ![]() Gene: aroA Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides Organism class: bacterialUniProt ID: P00780 ![]() Gene: apr Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 48. Fibroblast growth factor 1 Pharmacological action: unknownThe heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors Organism class: humanUniProt ID: P05230 ![]() Gene: FGF1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions Organism class: bacterialUniProt ID: P0A6K3 ![]() Gene: def Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: 50. Para-aminobenzoate synthase component 1 Pharmacological action: unknownCatalyzes the biosynthesis of 4-amino-4-deoxychorismate (ADC) from chorismate and glutamine Organism class: bacterialUniProt ID: P05041 ![]() Gene: pabB Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Reversible hydration of carbon dioxide Organism class: humanUniProt ID: P00918 ![]() Gene: CA2 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References: |
| Transporters |
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1. Monocarboxylate transporter 4 Actions: substrateProton-linked monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate UniProt ID: O15427![]() Gene: SLC16A3 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
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