Not to be confused with cytosine, cystine, cytisine, or cytidine.
"Cys" redirects here. For other uses, see Cys (disambiguation).
| L-Cysteine |
|
|
|
|
|
Other names
2-Amino-3-sulfhydrylpropanoic acid
|
| Identifiers |
| CAS number |
52-90-4 Y,
52-89-1 (hydrochloride) |
| PubChem |
5862 |
| ChemSpider |
574 (Racemic) Y, 5653 (L-form) Y |
| UNII |
K848JZ4886 Y |
| EC-number |
200-158-2 |
| KEGG |
D00026 Y |
| ChEBI |
CHEBI:15356 Y |
| ChEMBL |
CHEMBL54943 Y |
| Jmol-3D images |
Image 1
Image 2 |
-
C([C@@H](C(=O)O)N)S
C(C(C(=O)O)N)S
|
-
InChI=1S/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6) Y
Key: XUJNEKJLAYXESH-UHFFFAOYSA-N Y
InChI=1/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1
Key: XUJNEKJLAYXESH-REOHCLBHBU
InChI=1/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)
Key: XUJNEKJLAYXESH-UHFFFAOYAC
|
| Properties[2] |
| Molecular formula |
C3H7NO2S |
| Molar mass |
121.16 g mol−1 |
| Appearance |
white crystals or powder |
| Melting point |
240 °C decomp. |
| Solubility in water |
soluble |
| Solubility |
1.5g/100g ethanol 19 degC [1] |
| Chiral rotation [α]D |
+9.4° (H2O, c = 1.3) |
| Supplementary data page |
Structure and
properties |
n, εr, etc. |
Thermodynamic
data |
Phase behaviour
Solid, liquid, gas |
| Spectral data |
UV, IR, NMR, MS |
| Except where noted otherwise, data are given for materials in their standard state (at 25 °C (77 °F), 100 kPa) |
| Y (verify) (what is: Y/N?) |
| Infobox references |
|
|
Cysteine (abbreviated as Cys or C)[3] is an α-amino acid with the chemical formula HO2CCH(NH2)CH2SH. It is a semi-essential amino acid, which means that it can be biosynthesized in humans.[4] The thiol side chain in cysteine often participates in enzymatic reactions, serving as a nucleophile. The thiol is susceptible to oxidization to give the disulfide derivative cystine, which serves an important structural role in many proteins. When used as a food additive, it has the E number E920.
Contents
- 1 Sources
- 1.1 Dietary sources
- 1.2 Industrial sources
- 1.3 Biosynthesis
- 2 Biological functions
- 2.1 Precursor to the antioxidant glutathione
- 2.2 Precursor to iron-sulfur clusters
- 2.3 Metal ion binding
- 2.4 Roles in protein structure
- 3 Applications
- 3.1 Reducing toxic effects of alcohol
- 3.2 N-Acetylcysteine
- 4 Sheep
- 5 See also
- 6 References
- 7 External links
Sources
Dietary sources
Although classified as a non-essential amino acid, in rare cases, cysteine may be essential for infants, the elderly, and individuals with certain metabolic disease or who suffer from malabsorption syndromes. Cysteine can usually be synthesized by the human body under normal physiological conditions if a sufficient quantity of methionine is available. Cysteine is catabolized in the gastrointestinal tract and blood plasma[citation needed]. In contrast, cystine travels safely through the GI tract and blood plasma and is promptly reduced to the two cysteine molecules upon cell entry.[citation needed]
Cysteine is found in most high-protein foods, including:
- Animal sources: pork, poultry, eggs, dairy
- Plant sources: red peppers, garlic, onions, broccoli, brussels sprout, oats, granola, wheat germ, sprouted lentils.[5][6][unreliable source?]
Like other amino acids, cysteine has an amphoteric character.
(
R)-Cysteine (left) and (
S)-Cysteine (right) in zwitterionic form at neutral pH
Industrial sources
The majority of L-cysteine is obtained industrially by hydrolysis of poultry feathers or human hair.[7] Synthetically produced L-cysteine, compliant with Jewish Kosher and Muslim Halal laws, is also available, albeit at a higher price.[8] The synthetic route involves fermentation using a mutant of E. coli. Degussa introduced a route from substituted thiazolines.[9] Following this technology, L-cysteine is produced by the hydrolysis of racemic 2-amino-Δ2-thiazoline-4-carboxylic acid using Pseudomonas thiazolinophilum.[10]
Biosynthesis
Cysteine synthesis. Cystathionine beta synthase catalyzes the upper reaction and cystathionine gamma-lyase catalyzes the lower reaction.
In animals, biosynthesis begins with the amino acid serine. The sulfur is derived from methionine, which is converted to homocysteine through the intermediate S-adenosylmethionine. Cystathionine beta-synthase then combines homocysteine and serine to form the asymmetrical thioether cystathionine. The enzyme cystathionine gamma-lyase converts the cystathionine into cysteine and alpha-ketobutyrate. In plants and bacteria, cysteine biosynthesis again starts from serine, which is converted to O-acetylserine by the enzyme serine transacetylase. The enzyme O-acetylserine (thiol)-lyase, using sulfide sources, converts this ester into cysteine, releasing acetate.[11]
Biological functions
The cysteine thiol group is nucleophilic and easily oxidized. The reactivity is enhanced when the thiol is ionized, and cysteine residues in proteins have pKa values close to neutrality, so are often in their reactive thiolate form in the cell.[12] Because of its high reactivity, the thiol group of cysteine has numerous biological functions.
Precursor to the antioxidant glutathione
Due to the ability of thiols to undergo redox reactions, cysteine has antioxidant properties. Cysteine's antioxidant properties are typically expressed in the tripeptide glutathione, which occurs in humans as well as other organisms. The systemic availability of oral glutathione (GSH) is negligible; so it must be biosynthesized from its constituent amino acids, cysteine, glycine, and glutamic acid. Glutamic acid and glycine are readily available in most Western diets, but the availability of cysteine can be the limiting substrate.[citation needed]
Precursor to iron-sulfur clusters
Cysteine is an important source of sulfide in human metabolism. The sulfide in iron-sulfur clusters and in nitrogenase is extracted from cysteine, which is converted to alanine in the process.[13]
Metal ion binding
Beyond the iron-sulfur proteins, many other metal cofactors in enzymes are bound to the thiolate substituent of cysteinyl residues. Examples include zinc in zinc fingers and alcohol dehydrogenase, copper in the blue copper proteins, iron in cytochrome P450, and nickel in the [NiFe]-hydrogenases.[14] The thiol group also has a high affinity for heavy metals, so that proteins containing cysteine, such as metallothionein, will bind metals such as mercury, lead, and cadmium tightly.[15]
Roles in protein structure
In the translation of messenger RNA molecules to produce polypeptides, cysteine is coded for by the UGU and UGC codons.
Cysteine has traditionally been considered to be a hydrophilic amino acid, based largely on the chemical parallel between its thiol group and the hydroxyl groups in the side-chains of other polar amino acids. However, the cysteine side chain has been shown to stabilize hydrophobic interactions in micelles to a greater degree than the side chain in the non-polar amino acid glycine, and the polar amino acid serine.[16] In a statistical analysis of the frequency with which amino acids appear in different chemical environments in the structures of proteins, free cysteine residues were found to associate with hydrophobic regions of proteins. Their hydrophobic tendency was equivalent to that of known non-polar amino acids such as methionine and tyrosine, and was much greater than that of known polar amino acids such as serine and threonine.[17] Hydrophobicity scales, which rank amino acids from most hydrophobic to most hydrophilic, consistently place cysteine towards the hydrophobic end of the spectrum, even when they are based on methods that are not influenced by the tendency of cysteines to form disulfide bonds in proteins. Therefore, cysteine is now often grouped among the hydrophobic amino acids,[18][19] though it is sometimes also classified as slightly polar,[20] or polar.[4]
While free cysteine residues do occur in proteins, most are covalently bonded to other cysteine residues to form disulfide bonds. Disulfide bonds play an important role in the folding and stability of some proteins, usually proteins secreted to the extracellular medium.[21] Since most cellular compartments are reducing environments, disulfide bonds are generally unstable in the cytosol with some exceptions as noted below.
Figure 2: Cystine (shown here in its neutral form), two cysteines bound together by a disulfide bond.
Disulfide bonds in proteins are formed by oxidation of the thiol groups of cysteine residues. The other sulfur-containing amino acid, methionine, cannot form disulfide bonds. More aggressive oxidants convert cysteine to the corresponding sulfinic acid and sulfonic acid. Cysteine residues play a valuable role by crosslinking proteins, which increases the rigidity of proteins and also functions to confer proteolytic resistance (since protein export is a costly process, minimizing its necessity is advantageous). Inside the cell, disulfide bridges between cysteine residues within a polypeptide support the protein's tertiary structure. Insulin is an example of a protein with cystine crosslinking, wherein two separate peptide chains are connected by a pair of disulfide bonds.
Protein disulfide isomerases catalyze the proper formation of disulfide bonds; the cell transfers dehydroascorbic acid to the endoplasmic reticulum, which oxidises the environment. In this environment, cysteines are, in general, oxidized to cystine and are no longer functional as a nucleophiles.
Aside from its oxidation to cystine, cysteine participates in numerous posttranslational modifications. The nucleophilic thiol group allows cysteine to conjugate to other groups, e.g., in prenylation. Ubiquitin ligases transfer ubiquitin to its pendant, proteins, and caspases, which engage in proteolysis in the apoptotic cycle. Inteins often function with the help of a catalytic cysteine. These roles are typically limited to the intracellular milieu, where the environment is reducing, and cysteine is not oxidized to cystine.
Applications
Cysteine, mainly the L-enantiomer, is a precursor in the food, pharmaceutical, and personal-care industries. One of the largest applications is the production of flavors. For example, the reaction of cysteine with sugars in a Maillard reaction yields meat flavors.[22] L-Cysteine is also used as a processing aid for baking.[23]
In the field of personal care, cysteine is used for permanent wave applications, predominantly in Asia. Again, the cysteine is used for breaking up the disulfide bonds in the hair's keratin.
Cysteine is a very popular target for site-directed labeling experiments to investigate biomolecular structure and dynamics. Maleimides will selectively attach to cysteine using a covalent Michael addition. Site-directed spin labeling for EPR or paramagnetic relaxation enhanced NMR also uses cysteine extensively.
In a 1994 report released by five top cigarette companies, cysteine is one of the 599 additives to cigarettes. Like most cigarette additives, however, its use or purpose is unknown.[24] Its inclusion in cigarettes could offer two benefits: acting as an expectorant, since smoking increases mucus production in the lungs; or increasing the beneficial antioxidant glutathione (which is diminished in smokers).
Reducing toxic effects of alcohol
Cysteine has been proposed as a preventative or antidote for some of the negative effects of alcohol, including liver damage and hangover. It counteracts the poisonous effects of acetaldehyde, which is the major byproduct of alcohol metabolism and is responsible for most of the negative after effects and long-term damage associated with alcohol use (but not the immediate effects of drunkenness). Cysteine supports the next step in metabolism, which turns acetaldehyde into the relatively harmless acetic acid. In a rat study, test animals received an LD50 dose of acetaldehyde. Those that received cysteine had an 80% survival rate; when both cysteine and thiamine were administered, all animals survived.[25] No direct evidence indicates its effectiveness in humans who consume alcohol at normal levels.
N-Acetylcysteine
N-Acetyl-L-cysteine is a derivative of cysteine wherein an acetyl group is attached to the nitrogen atom. This compound is sold as a dietary supplement, and used as an antidote in cases of acetaminophen overdose,[26] and obsessive compulsive disorders such as trichotillomania.
Sheep
Cysteine is required by sheep to produce wool: It is an essential amino acid that must be taken in from their feed. As a consequence, during drought conditions, sheep produce less wool; however, transgenic sheep that can make their own cysteine have been developed.[27]
See also
- Amino acids
- Cysteine metabolism
- Cystinuria
- Selenocysteine
- Thiols
- Sullivan reaction
References
- ^ Belitz, H.-D; Grosch, Werner; Schieberle, Peter (2009-02-27). Food Chemistry. ISBN 9783540699330
- ^ Weast, Robert C., ed. (1981). CRC Handbook of Chemistry and Physics (62nd ed.). Boca Raton, FL: CRC Press. p. C-259. ISBN 0-8493-0462-8. .
- ^ "Nomenclature and symbolism for amino acids and peptides (IUPAC-IUB Recommendations 1983)", Pure Appl. Chem. 56 (5), 1984: 595–624, doi:10.1351/pac198456050595
- ^ a b "The primary structure of proteins is the amino acid sequence". The Microbial World. University of Wisconsin-Madison Bacteriology Department. Retrieved 16 September 2012.
- ^ "Cysteine". University of Maryland Medical Center.
- ^ "Lentils, sprouted, raw". bitterpoison.com.
- ^ Carney, Scott (April/March 2010 Issue). "The Temple of Do". Mother Jones. Retrieved 22 October 2012.
- ^ Questions About Food Ingredients: What is L-cysteine/cysteine/cystine?. Vegetarian Resource Group.
- ^ Martens, Jürgen; Offermanns, Heribert; Scherberich, Paul (1981). "Facile Synthesis of Racemic Cysteine". Angewandte Chemie International Edition in English 20 (8): 668. doi:10.1002/anie.198106681.
- ^ Drauz, Karlheinz; Grayson, Ian; Kleemann, Axel; Krimmer, Hans-Peter; Leuchtenberger, Wolfgang; Weckbecker, Christoph (2007). "Amino Acids". Ullmann's Encyclopedia of Industrial Chemistry. doi:10.1002/14356007.a02_057.pub2. ISBN 3-527-30673-0.
- ^ Hell R (1997). "Molecular physiology of plant sulfur metabolism". Planta 202 (2): 138–48. doi:10.1007/s004250050112. PMID 9202491.
- ^ Bulaj G, Kortemme T, Goldenberg DP (June 1998). "Ionization-reactivity relationships for cysteine thiols in polypeptides". Biochemistry 37 (25): 8965–72. doi:10.1021/bi973101r. PMID 9636038.
- ^ Lill R, Mühlenhoff U (2006). "Iron-sulfur protein biogenesis in eukaryotes: components and mechanisms". Annu. Rev. Cell Dev. Biol. 22: 457–86. doi:10.1146/annurev.cellbio.22.010305.104538. PMID 16824008.
- ^ Lippard, Stephen J.; Berg, Jeremy M. (1994). Principles of Bioinorganic Chemistry. Mill Valley, CA: University Science Books. ISBN 0-935702-73-3. [page needed]
- ^ Baker DH, Czarnecki-Maulden GL (June 1987). "Pharmacologic role of cysteine in ameliorating or exacerbating mineral toxicities". J. Nutr. 117 (6): 1003–10. PMID 3298579.
- ^ Heitmann P (January 1968). "A model for sulfhydryl groups in proteins. Hydrophobic interactions of the cystein side chain in micelles". Eur. J. Biochem. 3 (3): 346–50. doi:10.1111/j.1432-1033.1968.tb19535.x. PMID 5650851.
- ^ Nagano N, Ota M, Nishikawa K (September 1999). "Strong hydrophobic nature of cysteine residues in proteins". FEBS Lett. 458 (1): 69–71. doi:10.1016/S0014-5793(99)01122-9. PMID 10518936.
- ^ Betts, M.J.; R.B. Russell (2003). "Hydrophobic amino acids". Amino Acid Properties and Consequences of Substitutions, In: Bioinformatics for Geneticists. Wiley. Retrieved 2012-09-16.
- ^ Gorga, Frank R. (1998–2001). "Introduction to Protein Structure--Non-Polar Amino Acids". Retrieved 2012-09-16.
- ^ "Virtual Chembook--Amino Acid Structure". Elmhurst College. Retrieved 2012-09-16.
- ^ Sevier CS, Kaiser CA (November 2002). "Formation and transfer of disulphide bonds in living cells". Nat. Rev. Mol. Cell Biol. 3 (11): 836–47. doi:10.1038/nrm954. PMID 12415301.
- ^ Huang, Tzou-Chi; Ho, Chi-Tang. "Flavors of Meat Products". In Hui, Y. H.; Nip, Wai-Kit; Rogers, Robert. Meat Science and Applications. CRC. pp. 71–102. ISBN 978-0-203-90808-2.
- ^ Food Ingredients and Colors. U.S. Food and Drug Administration. November 2004. Retrieved 2009-09-06 .
- ^ Martin, Terry (2009-06-25). "The List of Additives in Cigarettes". about.com. Retrieved 2009-09-06. .
- ^ Sprince H, Parker CM, Smith GG, Gonzales LJ (April 1974). "Protection against acetaldehyde toxicity in the rat by L-cysteine, thiamin and L-2-methylthiazolidine-4-carboxylic acid". Agents Actions 4 (2): 125–30. doi:10.1007/BF01966822. PMID 4842541.
- ^ Kanter MZ (October 2006). "Comparison of oral and i.v. acetylcysteine in the treatment of acetaminophen poisoning". Am J Health Syst Pharm 63 (19): 1821–7. doi:10.2146/ajhp060050. PMID 16990628.
- ^ Powell BC, Walker SK, Bawden CS, Sivaprasad AV, Rogers GE (1994). "Transgenic sheep and wool growth: possibilities and current status". Reprod. Fertil. Dev. 6 (5): 615–23. doi:10.1071/RD9940615. PMID 7569041.
External links
- Cysteine MS Spectrum
- International Kidney Stone Institute
- http://www.chemie.fu-berlin.de/chemistry/bio/aminoacid/cystein en.html
- Nagano N, Ota M, Nishikawa K (September 1999). "Strong hydrophobic nature of cysteine residues in proteins". FEBS Lett. 458 (1): 69–71. doi:10.1016/S0014-5793(99)01122-9. PMID 10518936.
- 952-10-3056-9 Interaction of alcohol and smoking in the pathogenesis of upper digestive tract cancers - possible chemoprevention with cysteine
- Cystine Kidney Stones
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Cough and cold preparations (R05)
|
|
| Expectorants |
- Althea root
- Antimony pentasulfide
- Creosote
- Guaiacolsulfonate
- Guaifenesin
- Ipecacuanha (Syrup of ipecac)
- Levoverbenone
- Potassium iodide
- Senega
- Tyloxapol
- Ammonium Chloride
|
|
| Mucolytics |
- Acetylcysteine
- Ambroxol
- Bromhexine
- Carbocisteine
- Domiodol
- Dornase alfa
- Eprazinone
- Erdosteine
- Letosteine
- Mannitol
- Mesna
- Neltenexine
- Sobrerol
- Stepronin
- Tiopronin
|
|
| Cough suppressants |
Opium alkaloids,
opioids,
and derivatives |
- Acetyldihydrocodeine
- Benzylmorphine
- Butorphanol
- Codeine
- Dextromethorphan
- Diacetylmorphine
- Dihydrocodeine
- Dimemorfan
- Droxypropine
- Ethylmorphine
- Hydrocodone
- Hydromorphone
- Isoaminile
- Laudanum
- Levomethadone
- Levopropoxyphene
- Methadone
- Nicocodeine
- Nicodicodeine
- Normethadone
- Noscapine
- Pholcodine
- Thebacon
- Tipepidine
|
|
|
Other
|
- Benzonatate
- Benproperine
- Bibenzonium bromide
- Butamirate
- Clobutinol
- Clofedanol
- Cloperastine
- Diphenhydramine
- Dibunate
- Dimethoxanate
- Dropropizine
- Fedrilate
- Glaucine
- Levodropropizine
- Meprotixol
- Morclofone
- Nepinalone
- Oxolamine
- Oxeladin
- Pentoxyverine
- Pipazetate
- Prenoxdiazine
- Piperidione
- Zipeprol
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anat (n, x, l, c)/phys/devp
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noco (c, p)/cong/tumr, sysi/epon, injr
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proc, drug (R1/2/3/5/6/7)
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|
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Antidotes (V03AB)
|
|
Nervous
system |
Nerve agent /
Organophosphate
poisoning |
- Atropine#
- Biperiden
- Diazepam#
- Oximes
- see also: Cholinesterase
|
|
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Barbiturate
overdose
|
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Benzodiazepine
overdose
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GHB overdose
|
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Opioid overdose
|
- Diprenorphine
- Doxapram
- Nalmefene
- Nalorphine
- Naloxone#
- Naltrexone
|
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Reversal of
neuromuscular blockade
|
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|
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Circulatory
system |
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Beta blocker
|
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Digoxin toxicity
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Heparin
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| Other |
|
Arsenic poisoning
|
|
|
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Cyanide poisoning
|
- 4-Dimethylaminophenol
- Hydroxocobalamin
- nitrite
- Amyl nitrite
- Sodium nitrite#
- Sodium thiosulfate#
|
|
|
Hydrofluoric acid
|
|
|
Methanol /
Ethylene glycol
poisoning |
|
|
|
Paracetamol toxicity
(Acetaminophen)
|
- Acetylcysteine#
- Glutathione
- Methionine#
|
|
|
|
- Dimercaprol#
- Edetates
- Prussian blue#
|
|
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Other
|
- iodine-131
- Methylthioninium chloride#
- oxidizing agent
- Prednisolone/promethazine
|
|
|
| Emetic |
- Copper sulfate
- Ipecacuanha
|
|
- #WHO-EM
- ‡Withdrawn from market
- Clinical trials:
- †Phase III
- §Never to phase III
|
|
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The 20 common amino acids
|
|
| General topics |
- Protein
- Peptide
- Genetic code
|
|
|
| By properties |
|
Aliphatic
|
- Branched-chain amino acids (Valine
- Isoleucine
- Leucine)
- Methionine
- Alanine
- Proline
- Glycine
|
|
|
Aromatic
|
- Phenylalanine
- Tyrosine
- Tryptophan
- Histidine
|
|
|
Polar, uncharged
|
- Asparagine
- Glutamine
- Serine
- Threonine
|
|
|
Positive charge (pKa)
|
- Lysine (≈10.8)
- Arginine (≈12.5)
- Histidine (≈6.1)
|
|
|
Negative charge (pKa)
|
- Aspartic acid (≈3.9)
- Glutamic acid (≈4.1)
- Cysteine (≈8.3)
- Tyrosine (≈10.1)
|
|
|
| Other classifications |
- Essential amino acid
- Ketogenic amino acid
- Glucogenic amino acid
- Non-proteinogenic amino acid
|
|
- Biochemical families: carbohydrates
- alcohols
- glycoproteins
- glycosides
- lipids
- eicosanoids
- fatty acids / intermediates
- phospholipids
- sphingolipids
- steroids
- nucleic acids
- constituents / intermediates
- proteins
- Amino acids / intermediates
- tetrapyrroles / intermediates
|
|
|
E numbers
|
|
- Colours (E100–199)
- Preservatives (E200–299)
- Antioxidants & acidity regulators (E300–399)
- Thickeners, stabilisers & emulsifiers (E400–499)
- pH regulators & anticaking agents (E500–599)
- Flavour enhancers (E600–699)
- Miscellaneous (E900–999)
- Additional chemicals (E1100–1599)
- Waxes (E900–909)
- Synthetic glazes (E910–919)
- Improving agents (E920–929)
- Packaging gases (E930–949)
- Sweeteners (E950–969)
- Foaming agents (E990–999)
- L-cysteine (E920)
- L-cystine (E921)
- Potassium persulfate (E922)
- Ammonium persulfate (E923)
- Potassium bromate (E924)
- Chlorine (E925)
- Chlorine dioxide (E926)
- Azodicarbonamide (E927)
- Carbamide (E927b)
- Benzoyl peroxide (E928)
|
|
|
Amino acid metabolism metabolic intermediates
|
|
| K→acetyl-CoA |
|
lysine→
|
- Saccharopine
- Allysine
- α-Aminoadipic acid
- α-Aminoadipate
- Glutaryl-CoA
- Glutaconyl-CoA
- Crotonyl-CoA
- β-Hydroxybutyryl-CoA
|
|
|
leucine→
|
- α-Ketoisocaproic acid
- Isovaleryl-CoA
- 3-Methylcrotonyl-CoA
- 3-Methylglutaconyl-CoA
- HMG-CoA
|
|
|
tryptophan→alanine→
|
- N'-Formylkynurenine
- Kynurenine
- Anthranilic acid
- 3-Hydroxykynurenine
- 3-Hydroxyanthranilic acid
- 2-Amino-3-carboxymuconic semialdehyde
- 2-Aminomuconic semialdehyde
- 2-Aminomuconic acid
- Glutaryl-CoA
|
|
|
| G |
|
G→pyruvate→citrate
|
|
glycine→serine→
|
- glycine→creatine: Glycocyamine
- Phosphocreatine
- Creatinine
|
|
|
|
G→glutamate→
α-ketoglutarate
|
|
histidine→
|
- Urocanic acid
- Imidazol-4-one-5-propionic acid
- Formiminoglutamic acid
- Glutamate-1-semialdehyde
|
|
|
proline→
|
- 1-Pyrroline-5-carboxylic acid
|
|
|
arginine→
|
- Ornithine
- Putrescine
- Agmatine
|
|
|
other
|
- cysteine+glutamate→glutathione: γ-Glutamylcysteine
|
|
|
|
G→propionyl-CoA→
succinyl-CoA
|
|
valine→
|
- α-Ketoisovaleric acid
- Isobutyryl-CoA
- Methacrylyl-CoA
- 3-Hydroxyisobutyryl-CoA
- 3-Hydroxyisobutyric acid
- 2-Methyl-3-oxopropanoic acid
|
|
|
isoleucine→
|
- 2,3-Dihydroxy-3-methylpentanoic acid
- 2-Methylbutyryl-CoA
- Tiglyl-CoA
- 2-Methylacetoacetyl-CoA
|
|
|
methionine→
|
- generation of homocysteine: S-Adenosyl methionine
- S-Adenosyl-L-homocysteine
- Homocysteine
- conversion to cysteine: Cystathionine
- alpha-Ketobutyric acid+Cysteine
|
|
|
threonine→
|
|
|
|
propionyl-CoA→
|
|
|
|
|
G→fumarate
|
|
phenylalanine→tyrosine→
|
- 4-Hydroxyphenylpyruvic acid
- Homogentisic acid
- 4-Maleylacetoacetic acid
|
|
|
|
G→oxaloacetate
|
|
|
|
| Other |
|
|
|
|
mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m
|
k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon
|
m (A16/C10), i (k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)
|
|
- Biochemical families: carbohydrates
- alcohols
- glycoproteins
- glycosides
- lipids
- eicosanoids
- fatty acids / intermediates
- phospholipids
- sphingolipids
- steroids
- nucleic acids
- constituents / intermediates
- proteins
- Amino acids / intermediates
- tetrapyrroles / intermediates
|
|
