L-isoleucine

L-isoleucine is one of the essential alpha-amino acids crucial for protein biosynthesis, with its abbreviation in the IUPAC-IUBMB nomenclature as Ile or I. It is among the 20 primary amino acids encoded by the human genome, excluding Selenocysteine. Unlike non-essential amino acids, L-isoleucine cannot be synthesized de novo by cells, making its dietary intake critical for proper bodily function.

It is coded by mRNA using the codons AUU, AUC, and AUA, forming an aliphatic hydrophobic residue within proteins. In terms of its catabolism in humans, L-isoleucine serves as a mixed amino acid. It can serve as both a ketoacid precursor for glucose, traversing the Krebs cycle and gluconeogenesis, and contribute to ketone body formation through the transformation of acetyl-CoA to Acetoacetyl-CoA, subsequently joining the ketogenesis pathway.

This amino acid plays an integral role in the ketone body pathway (ketogenesis) and in gluconeogenesis to produce the necessary energy required for maintaining a balanced metabolism.

L-isoleucine is an essential branched-chain aliphatic amino acid, meaning it cannot be synthesized by the human body and must be obtained from the diet. It is one of the 20 standard amino acids that are the building blocks of proteins. Encoded by the codons AUU, AUC, and AUA, it is an important component in the process of protein biosynthesis. Its molecular formula is C6H13NO2.

L-isoleucine is known for its role in the regulation of blood sugar levels, muscle metabolism, and immune function. It plays a key role in the stimulation of muscle protein synthesis and the prevention of muscle breakdown during exercise. Additionally, it is involved in the production and maintenance of energy, as well as the formation of hemoglobin.

Food sources rich in L-isoleucine include various animal products, such as meat, fish, eggs, and dairy, as well as certain plant-based proteins like legumes, seeds, and nuts. It is often found in high-protein foods and is a common component of dietary supplements aimed at promoting muscle growth and recovery.

 

MBS358067 | Polyclonal anti-conjugated L-isoleucine antibodies
MBS358325 | L-Isoleucine (BSA) conjugate
MBS405259 | L-Isoleucine
MBS545703 | L-ISOLEUCINE
MBS649825 | L-Isoleucine, Conjugated
MBS651560 | Enniatin B1 (2-(N-Methyl-L-isoleucine) Enniatin B)
MBS653278 | RPMI 1640 Medium Deficient w/L-Glutamine, w/o Isoleucine (Powder)
MBS6105036 | L-Isoleucine
MBS3608795 | (4S)-4-Hydroxy-L-isoleucine
MBS3609988 | L-allo-Isoleucine
MBS4158167 | Anti-Conjugated L-Isoleucine Antibody
MBS5750187 | (4S)-4-Hydroxy-L-isoleucine


Accession Number : KLM0000241 This work is released into the public domain; please see our release statement.

Synonyms :

L-ISOLEUCINE
Ile
I
Config Rule :

config('L-isoleucine',[
substituent(aminoacid_L_backbone),
substituent(methylpropyl),
linkage(from(aminoacid_L_backbone,car(1)),
to(methylpropyl,car(1)),
down,single)]).

%%%% Substituent Config Rules for compound 'L-isoleucine' %%%%

config(aminoacid_L_backbone,[
left(amino),
right(hyd),
top(carboxyl),
center(car(1))]).

config(methylpropyl,[
top(car(1,methyl&&hyd;)),
center(methandiyl),
bottom(methyl(3))]).

Smiles String :

[C@2H]([NH3+])([C](=[O])[O-])[C@2H]([CH3])[C@2H2][CH3]

'L-isoleucine'

Fischer Diagram :


Terminal :

% 'L-isoleucine'

c(1,12,(0,chiral))-[n(1,left)~,h(1,right)~,c(2,up)~,c(3,down)~],
c(2,12,(0,nonchiral))-[o(1,nil)?,o(2,nil)?,c(1,down)~],
c(3,12,(0,chiral))-[c(4,left)~,c(6,right)~,c(1,up)~,h(7,down)~],
c(4,12,(0,nonchiral))-[c(5,left)~,c(3,right)~,h(5,up)~,h(6,down)~],
c(5,12,(0,nonchiral))-[h(11,left)~,c(4,right)~,h(12,up)~,h(13,down)~],
c(6,12,(0,nonchiral))-[c(3,left)~,h(8,right)~,h(10,up)~,h(9,down)~],
h(1,1,(0,nonchiral))-[c(1,left)~],
h(2,1,(0,nonchiral))-[n(1,right)~],
h(3,1,(0,nonchiral))-[n(1,down)~],
h(4,1,(0,nonchiral))-[n(1,up)~],
h(5,1,(0,nonchiral))-[c(4,down)~],
h(6,1,(0,nonchiral))-[c(4,up)~],
h(7,1,(0,nonchiral))-[c(3,up)~],
h(8,1,(0,nonchiral))-[c(6,left)~],
h(9,1,(0,nonchiral))-[c(6,up)~],
h(10,1,(0,nonchiral))-[c(6,down)~],
h(11,1,(0,nonchiral))-[c(5,right)~],
h(12,1,(0,nonchiral))-[c(5,down)~],
h(13,1,(0,nonchiral))-[c(5,up)~],
n(1,14,(1,nonchiral))-[h(2,left)~,c(1,right)~,h(3,up)~,h(4,down)~],
o(1,16,(-5.0E-01,nonchiral))-[c(2,nil)?],
o(2,16,(-5.0E-01,nonchiral))-[c(2,nil)?]

The Terminals for all the Config Rules are in Prolog Definite Clause Grammar (DCG) form.They can be checked in the Manual here.

The compound's PDB file can be seen here.