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Alloisoleucine

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Alloisoleucine
Identifiers
3D model (JSmol)
1721791
ChEBI
ChEMBL
ChemSpider
DrugBank
ECHA InfoCard 100.014.676 Edit this at Wikidata
EC Number
  • L-enantiomer: 216-142-3
  • racemic: 207-139-8
UNII
  • InChI=1S/C6H13NO2/c1-3-4(2)5(7)6(8)9/h4-5H,3,7H2,1-2H3,(H,8,9)/t4-,5+/m1/s1
    Key: AGPKZVBTJJNPAG-UHNVWZDZSA-N
  • D enantiomer: 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
    Key: AGPKZVBTJJNPAG-CRCLSJGQSA-N
  • L-enantiomer: CC[C@@H](C)[C@@H](C(=O)O)N
  • D enantiomer: CC[C@H](C)[C@H](C(=O)O)N
  • racemic: CCC(C)C(C(=O)O)N
Properties
Appearance white solid
Melting point 285 °C (545 °F; 558 K)
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).

Alloisoleucine is an amino acid with the formula CH3CH2CH(CH3)CH(NH2)CO2H. It exists as two enantiomers, of which the L derivative occurs naturally. L-Alloisoleucine occurs in healthy serum in only trace amounts, except for individuals suffering from maple syrup urine disease.[1]

Structure

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Together with valine, leucine, and isoleucine, alloisoleucine is classified as a branched-chain amino acid (BCAA). It is the rarest of the four.

L-Alloisoleucine is a diastereomer of the proteogenic amino acid L-isoleucine. The stereochemistry of the isobutyl group differs for L-alloisoleucine and L-isoleucine.

 
l-isoleucine (2S,3S) and d-isoleucine (2R,3R)
 
l-alloisoleucine (2S,3R) and d-alloisoleucine (2R,3S)

Role in biosynthesis

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L-allo-isoleucine is a precursor to coronamic acid, which is a constituent of the phytotoxin coronatine, produced by Pseudomonas syringae.[2]

References

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  1. ^ Schadewaldt, Peter; Bodner-Leidecker, Annette; Hammen, Hans-Werner; Wendel, Udo (2000). "Formation of L-Alloisoleucine in Vivo : An L-[13C]Isoleucine Study in Man". Pediatric Research. 47 (2): 271–277. doi:10.1203/00006450-200002000-00020. PMID 10674358. S2CID 530588.
  2. ^ Vaillancourt, Frédéric H.; Yeh, Ellen; Vosburg, David A.; O'Connor, Sarah E.; Walsh, Christopher T. (August 2005). "Cryptic chlorination by a non-haem iron enzyme during cyclopropyl amino acid biosynthesis". Nature. 436 (7054): 1191–1194. Bibcode:2005Natur.436.1191V. doi:10.1038/nature03797. ISSN 1476-4687. PMID 16121186. S2CID 4428247.