Alloisoleucine

Alloisoleucine
Identifiers
CAS Number	L: 1509-35-8; D: 1509-34-9; racemic: 3107-04-8;
3D model (JSmol)	L: Interactive image; D: Interactive image; racemic: Interactive image;
Beilstein Reference	1721791
ChEBI	L: CHEBI:43433; D: CHEBI:20899;
ChEMBL	L: ChEMBL56053;
ChemSpider	L: 89698; D: 85019;
DrugBank	L: DB01739;
ECHA InfoCard	100.014.676
EC Number	L: 216-142-3; racemic: 207-139-8;
PubChem CID	L: 99288; D: 94206;
UNII	L: 6RNR8XN7S2; racemic: 05T3WT3PJ1;
CompTox Dashboard (EPA)	L: DTXSID901019590 ;
	InChI 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: 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;
	SMILES L: CC[C@@H](C)[C@@H](C(=O)O)N; D: CC[C@H](C)[C@H](C(=O)O)N; racemic: CCC(C)C(C(=O)O)N;
Properties
Chemical formula	C6H13NO2
Molar mass	131.175 g·mol−1
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). Infobox references

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

Structure

Together with valine, leucine, and isoleucine, alloisoleucine is classified as a branched-chain amino acid (BCAA). The L enantiomer of valine, leucine, and isoleucine are proteinogenic amino acids; alloisoleucine is non-proteinogenic.


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

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

Role in biosynthesis

L-Alloisoleucine is a precursor to coronatine, a phytotoxin produced by Pseudomonas syringae.^[2]

References

^ 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.
^ 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.

[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.

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