Isoleucine

Source: Wikipedia, the free encyclopedia.
l-Isoleucine
Chemical structure of Isoleucine
Skeletal formula of L-isoleucine
Ball-and-stick model of L-isoleucine
Ball-and-stick model of L-isoleucine
Space-filling model of L-isoleucine
Space-filling model of L-isoleucine
Names
IUPAC name
Isoleucine
Other names
(2S,3S)-2-amino-3-methylpentanoic acid
Identifiers
3D model (
JSmol
)
ChEBI
ChemSpider
DrugBank
ECHA InfoCard
 100.000.726 Edit this at Wikidata
IUPHAR/BPS
KEGG
UNII
  • InChI=1S/C6H13NO2/c1-3-4(2)5(7)6(8)9/h4-5H,3,7H2,1-2H3,(H,8,9)/t4-,5-/m0/s1 checkY
    Key: AGPKZVBTJJNPAG-WHFBIAKZSA-N checkY
  • InChI=1/C6H13NO2/c1-3-4(2)5(7)6(8)9/h4-5H,3,7H2,1-2H3,(H,8,9)/t4-,5-/m0/s1
    Key: AGPKZVBTJJNPAG-WHFBIAKZBB
  • CC[C@H](C)[C@@H](C(=O)O)N
  • Zwitterion: CC[C@H](C)[C@@H](C(=O)[O-])[NH3+]
Properties
C6H13NO2
Molar mass 131.175 g·mol−1
−84.9·10−6 cm3/mol
Supplementary data page
Isoleucine (data page)
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
checkY verify (what is checkY☒N ?)

Isoleucine (symbol Ile or I)

codons
AUU, AUC, and AUA.

Metabolism

Biosynthesis

In plants and microorganisms, isoleucine is synthesized from

alpha-ketobutyrate. This pathway is not present in humans. Enzymes involved in this biosynthesis include:[4]

  1. Acetolactate synthase (also known as acetohydroxy acid synthase)
  2. Acetohydroxy acid isomeroreductase
  3. Dihydroxyacid dehydratase
  4. Valine aminotransferase

Catabolism

Isoleucine is both a

ketone bodies (hence ketogenic) or fatty acids.[5]

Metabolic diseases

The degradation of isoleucine is impaired in the following metabolic diseases:

Insulin resistance

Isoleucine, like other branched-chain amino acids, is associated with insulin resistance: higher levels of isoleucine are observed in the blood of diabetic mice, rats, and humans.[6] In diet-induced obese and insulin resistant mice, a diet with decreased levels of isoleucine (with or without the other branched-chain amino acids) results in reduced adiposity and improved insulin sensitivity.[7][8] Reduced dietary levels of isoleucine are required for the beneficial metabolic effects of a low protein diet.[8] In humans, a protein restricted diet lowers blood levels of isoleucine and decreases fasting blood glucose levels.[9] Mice fed a low isoleucine diet are leaner, live longer, and are less frail.[10] In humans, higher dietary levels of isoleucine are associated with greater body mass index.[8]

Functions and requirement

The Food and Nutrition Board (FNB) of the U.S. Institute of Medicine has set Recommended Dietary Allowances (RDAs) for essential amino acids in 2002. For adults 19 years and older, 19 mg of isoleucine/kg body weight is required daily.[11]

Beside its biological role as a nutrient, isoleucine also participates in regulation of glucose metabolism.[5] Isoleucine is an essential component of many proteins. As an essential amino acid, isoleucine must be ingested or protein production in the cell will be disrupted. Fetal hemoglobin is one of the many proteins that require isoleucine.[12] Isoleucine is present in the gamma chain of fetal hemoglobin and must be present for the protein to form. [12]

Genetic diseases can change the consumption requirements of isoleucine. Amino acids cannot be stored in the body. Buildup of excess amino acids will cause a buildup of toxic molecules so, humans have many pathways to degrade each amino acid when the need for protein synthesis has been met.[13] Mutations in isoleucine-degrading enzymes can lead to dangerous buildup of isoleucine and its toxic derivative. One example is maple syrup urine disease (MSUD), a disorder that leaves people unable to breakdown isoleucine, valine, and leucine.[14] People with MSUD manage their disease by a reduced intake of all three of those amino acids alongside drugs that help excrete built-up toxins. [15]

Many animals and plants are dietary sources of isoleucine as a component of proteins.

eggs, soy protein, seaweed, turkey, chicken, lamb, cheese, and fish
.

Synthesis

Routes to isoleucine are numerous. One common multistep procedure starts from

diethylmalonate.[16] Synthetic isoleucine was first reported in 1905 by French chemists Bouveault and Locquin.[17]

Discovery

German chemist Felix Ehrlich discovered isoleucine while studying the composition of beet-sugar molasses 1903.[18] In 1907 Ehrlich carried out further studies on fibrin, egg albumin, gluten, and beef muscle in 1907. These studies verified the natural composition of isoleucine.[18] Ehrlich published his own synthesis of isoleucine in 1908. [19]

See also

References

  1. PMID 6743224
    .
  2. S2CID 22641155
    .
  3. PMID 142769
    .
  4. ^
    OCLC 42619569
    .
  5. ^
    OCLC 898999904
    .
  6. PMID 25287287
    .
  7. PMID 29266268
    .
  8. ^
    PMID 33887198
    .
  9. PMID 27346343
    .
  10. PMID 37939658
    .
  11. OCLC 57373786
    .
  12. ^
    PMID 4964832
    .
  13. PMID 16950638
    .
  14. PMID 32491705
    . Retrieved 2023-04-16.
  15. PMID 21098507
    .
  16. ISSN 0078-6209
    .
  17. ^ Bouvealt L, Locquin R (1905). "Sur la synthése d'une nouvelle leucine". Compt. Rend. (141): 115–117.
  18. ^
    ISSN 0009-2665
    .
  19. ISSN 0365-9496
    .

External links
Retrieved from "https://en.wikipedia.org/w/index.php?title=Isoleucine&oldid=1217121106"