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| Name | N-Formylmethionine | ||||||||||||||||||||||||||||||||||||||||||
| Accession Number | DB04464 (EXPT01455) | ||||||||||||||||||||||||||||||||||||||||||
| Type | small molecule | ||||||||||||||||||||||||||||||||||||||||||
| Groups | experimental | ||||||||||||||||||||||||||||||||||||||||||
| Description | Effective in the initiation of protein synthesis. The initiating methionine residue enters the ribosome as N-formylmethionyl tRNA. This process occurs in Escherichia coli and other bacteria as well as in the mitochondria of eucaryotic cells. [PubChem] |
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| Structure |
Download: MOL | SDF | SMILES | InChI Display: 2D Structure | 3D Structure |
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| Synonyms | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Salts | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Brand names | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Brand mixtures | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Categories | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| CAS number | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Weight |
Average: 177.221 Monoisotopic: 177.045963913 |
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| Chemical Formula | C6H11NO3S | ||||||||||||||||||||||||||||||||||||||||||
| InChI Key | InChIKey=PYUSHNKNPOHWEZ-YFKPBYRVSA-N | ||||||||||||||||||||||||||||||||||||||||||
| InChI |
InChI=1S/C6H11NO3S/c1-11-3-2-5(6(9)10)7-4-8/h4-5H,2-3H2,1H3,(H,7,8)(H,9,10)/t5-/m0/s1
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| IUPAC Name |
(2S)-2-formamido-4-(methylsulfanyl)butanoic acid
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| SMILES |
[H][C@@](CCSC)(NC=O)C(O)=O
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| Mass Spec | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Taxonomy | |||||||||||||||||||||||||||||||||||||||||||
| Kingdom | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Classes | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Substructures | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Pharmacology | |||||||||||||||||||||||||||||||||||||||||||
| Indication | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Pharmacodynamics | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Mechanism of action | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Absorption | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Volume of distribution | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Protein binding | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Metabolism | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Route of elimination | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Half life | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Clearance | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Toxicity | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| 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 | solid | ||||||||||||||||||||||||||||||||||||||||||
| Experimental Properties | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Predicted Properties |
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| References | |||||||||||||||||||||||||||||||||||||||||||
| 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 | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Interactions | |||||||||||||||||||||||||||||||||||||||||||
| Drug Interactions | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Food Interactions | Not Available | ||||||||||||||||||||||||||||||||||||||||||
| Targets |
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Pharmacological action: unknown
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine Organism class: bacterialUniProt ID: P0A6W9 ![]() Gene: gshA 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. Putative ATP-dependent Clp protease proteolytic subunit, mitochondrial Pharmacological action: unknownClp cleaves peptides in various proteins in a process that requires ATP hydrolysis. Clp may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates Organism class: humanUniProt ID: Q16740 ![]() Gene: CLPP Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
4. Geranylgeranyl transferase type-2 subunit alpha Pharmacological action: unknownCatalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to both cysteines in Rab proteins with an -XXCC, -XCXC and -CCXX C-terminal, such as RAB1A, RAB3A and RAB5A respectively Organism class: humanUniProt ID: Q92696 ![]() Gene: RABGGTA ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
5. Geranylgeranyl transferase type-2 subunit beta Pharmacological action: unknownCatalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to both cysteines in Rab proteins with an -XXCC, -XCXC and -CCXX C-terminal, such as RAB1A, RAB3A and RAB5A respectively Organism class: humanUniProt ID: P53611 ![]() Gene: RABGGTB ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
6. Photosynthetic reaction center cytochrome c subunit Pharmacological action: unknownThe reaction center of purple bacteria contain a tightly bound cytochrome molecule which re-reduces the photo oxidized primary electron donor Organism class: bacterialUniProt ID: P07173 ![]() Gene: pufC ![]() Protein Sequence: FASTA SNPs: SNPJam Report ![]() References:
7. Reaction center protein H chain Pharmacological action: unknownThe reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis Organism class: bacterialUniProt ID: P06008 ![]() Gene: puhA ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
8. Reaction center protein L chain Pharmacological action: unknownThe reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis Organism class: bacterialUniProt ID: P06009 ![]() Gene: pufL ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
9. Reaction center protein M chain Pharmacological action: unknownThe reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis Organism class: bacterialUniProt ID: P06010 ![]() Gene: pufM ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
10. Light-harvesting protein B-800/820 alpha chain Pharmacological action: unknownAntenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers Organism class: bacterialUniProt ID: P35089 ![]() Protein Sequence: FASTA References:
11. Light-harvesting protein B-800/820 beta chain Pharmacological action: unknownAntenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers Organism class: bacterialUniProt ID: P35094 ![]() Protein Sequence: FASTA References:
12. Light-harvesting protein B-800/850 alpha chain Pharmacological action: unknownAntenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers Organism class: bacterialUniProt ID: P26789 ![]() Protein Sequence: FASTA References:
13. Light-harvesting protein B-800/850 beta chain Pharmacological action: unknownAntenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers Organism class: bacterialUniProt ID: P26790 ![]() Protein Sequence: FASTA References:
14. Antithrombin-III Pharmacological action: unknownMost important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin Organism class: humanUniProt ID: P01008 ![]() Gene: SERPINC1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system Organism class: humanUniProt ID: P61769 ![]() Gene: B2M ![]() Protein Sequence: FASTA SNPs: SNPJam Report ![]() References:
16. NADH-ubiquinone oxidoreductase chain 1 Pharmacological action: unknownOrganism class: human UniProt ID: P03886 ![]() Gene: MT-ND1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
17. HLA class I histocompatibility antigen, B-27 alpha chain Pharmacological action: unknownInvolved in the presentation of foreign antigens to the immune system Organism class: humanUniProt ID: P03989 ![]() Gene: HLA-B ![]() Protein Sequence: FASTA SNPs: SNPJam Report ![]() References:
18. Respiratory nitrate reductase 1 alpha chain Pharmacological action: unknownThe nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction Organism class: bacterialUniProt ID: P09152 ![]() Gene: narG ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
19. Respiratory nitrate reductase 1 beta chain Pharmacological action: unknownThe nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit Organism class: bacterialUniProt ID: P11349 ![]() Gene: narH ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
20. Respiratory nitrate reductase 1 gamma chain Pharmacological action: unknownThe nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The gamma chain is a membrane-embedded heme-iron unit resembling cytochrome b, which transfers electrons from quinones to the beta subunit Organism class: bacterialUniProt ID: P11350 ![]() Gene: narI ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
21. Protein S100-G Pharmacological action: unknownOrganism class: human UniProt ID: P29377 ![]() Gene: S100G ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
22. Rubredoxin Pharmacological action: unknownElectron acceptor for cytoplasmic lactate dehydrogenase Organism class: bacterialUniProt ID: P00269 ![]() Gene: rub ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
23. Cytochrome c oxidase subunit 4 isoform 1, mitochondrial Pharmacological action: unknownThis protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport Organism class: humanUniProt ID: P13073 ![]() Gene: COX4I1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
24. Cytochrome c oxidase subunit 1 Pharmacological action: unknownCytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1- 3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B Organism class: humanUniProt ID: P00395 ![]() Gene: MT-CO1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
25. Cytochrome c oxidase subunit 2 Pharmacological action: unknownCytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1- 3 form the functional core of the enzyme complex. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1 Organism class: humanUniProt ID: P00403 ![]() Gene: MT-CO2 Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
26. Cytochrome c oxidase subunit 3 Pharmacological action: unknownSubunits I, II and III form the functional core of the enzyme complex Organism class: humanUniProt ID: P00414 ![]() Gene: MT-CO3 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
27. Cytochrome c oxidase subunit 5A, mitochondrial Pharmacological action: unknownThis is the heme A-containing chain of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport Organism class: humanUniProt ID: P20674 ![]() Gene: COX5A ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
28. Cytochrome c oxidase subunit 5B, mitochondrial Pharmacological action: unknownOrganism class: human UniProt ID: P10606 ![]() Gene: COX5B SNPs: SNPJam Report ![]() References:
29. Cytochrome c oxidase subunit 6C Pharmacological action: unknownThis protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport Organism class: humanUniProt ID: P09669 ![]() Gene: COX6C ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
30. Cytochrome c oxidase subunit 7B, mitochondrial Pharmacological action: unknownThis protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport Organism class: humanUniProt ID: P24311 ![]() Gene: COX7B ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
31. Cytochrome c oxidase subunit 7C, mitochondrial Pharmacological action: unknownThis protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport Organism class: humanUniProt ID: P15954 ![]() Gene: COX7C ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
32. Cytochrome c oxidase subunit 8A, mitochondrial Pharmacological action: unknownThis protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport Organism class: humanUniProt ID: P10176 ![]() Gene: COX8A ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
33. Cytochrome c oxidase subunit 6A2, mitochondrial Pharmacological action: unknownThis protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport Organism class: humanUniProt ID: Q02221 ![]() Gene: COX6A2 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
34. Cytochrome c oxidase subunit 6B1 Pharmacological action: unknownConnects the two COX monomers into the physiological dimeric form (By similarity) Organism class: humanUniProt ID: P14854 ![]() Gene: COX6B1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
35. Cytochrome c oxidase polypeptide 7A1, mitochondrial Pharmacological action: unknownThis protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport Organism class: humanUniProt ID: P24310 ![]() Gene: COX7A1 ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
36. Methionyl-tRNA formyltransferase Pharmacological action: unknownModifies the free amino group of the aminoacyl moiety of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by:(I) promoting its recognition by IF2 and (II) impairing its binding to EFTu-GTP Organism class: bacterialUniProt ID: P23882 ![]() Gene: fmt ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
37. 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:
38. Protein S100-B Pharmacological action: unknownWeakly binds calcium but binds zinc very tightly- distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase Organism class: humanUniProt ID: P04271 ![]() Gene: S100B ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
39. Delta-hemolysin Pharmacological action: unknownLyses erythrocytes and many other mammalian cells Organism class: bacterialUniProt ID: P0C1V1 ![]() Gene: hld ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
40. Polyubiquitin-C Pharmacological action: unknownOrganism class: human UniProt ID: P0CG48 ![]() Gene: UBC SNPs: SNPJam Report ![]() References:
Pharmacological action: unknown
ATP + H(2)O + H(+)(In) = ADP + phosphate + H(+)(Out) Organism class: bacterialUniProt ID: A5HEI4 ![]() Gene: atpH ![]() Protein Sequence: FASTA SNPs: SNPJam Report ![]() References:
42. Probable L-ascorbate-6-phosphate lactonase ulaG Pharmacological action: unknownProbably catalyzes the hydrolysis of L-ascorbate-6-P into 3-keto-L-gulonate-6-P. Is essential for L-ascorbate utilization under anaerobic conditions. Also shows phosphodiesterase activity, hydrolyzing phosphodiester bond in the artificial chromogenic substrate bis-p-nitrophenyl phosphate (bis- pNPP) Organism class: bacterialUniProt ID: P39300 ![]() Gene: ulaG ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
43. Immunoglobulin G-binding protein G Pharmacological action: unknownOrganism class: bacterial UniProt ID: P19909 ![]() Gene: spg ![]() Protein Sequence: FASTA Gene Sequence: FASTA SNPs: SNPJam Report ![]() References:
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