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Results for "

isoleucine

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  • Inhibitors & Agonists
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L-Isoleucine
isoleucine, Ile
T006373-32-5
L-Isoleucine (Ile) is an essential branched-chain aliphatic amino acid found in many proteins. It is an isomer of LEUCINE. It is important in hemoglobin synthesis and regulation of blood sugar and energy levels.
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D-Isoleucine
(R)-Isoleucine, (2R,3R)-2-Amino-3-methylpentanoic acid
T9143319-78-8
D-Isoleucine ((2R,3R)-2-Amino-3-methylpentanoic acid) is a selective activator of Asc-1 antiporter, which enhances long-term potentiation at the hippocampal CA1-CA3 via release of endogenous D-serine.
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(2S,3R,4S)-4-Hydroxyisoleucine
(4S)-4-Hydroxy-L-isoleucine, Hydroxyisoleucine
T2P291955399-93-4
(2S,3R,4S)-4-Hydroxyisoleucine (Hydroxyisoleucine) from fenugreek (Trigonella foenum-graecum) seeds is a potential insulinotropic (anti-diabetic) and anti-obesity amino acid that stimulates glucose-dependent insulin secretion from pancreatic cells, activates insulin receptor substrate-associated phosphoinositide 3 (PI3) kinase activity, and reduces plasma levels of triglycerides, free fatty acids, and cholesterol.
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L-Alloisoleucine
L-allo-Isoleucine, L(+)-Alloisoleucine, (3R)-LS-Isoleucine
T52191509-34-8
L-Alloisoleucine (L-allo-Isoleucine) is a branched chain amino acid and is a stereoisomer of L-isoleucine. It is a common constituent of human plasma (albeit at low levels). L-alloisoleucine is produced as a byproduct of isoleucine transamination. Plasma L-alloisoleucine, which is derived from L-isoleucine in vivo, can be used for the diagnosis of maple syrup urine disease (MSUD), a genetic disorder. Indeed, plasma L-alloisoleucine levels above 5 μmol L is the most specific and most sensitive diagnostic marker for all forms of MSUD.
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4-Hydroxyisoleucine
4-​Hydroxy-​L-​isoleucine
T7448781658-23-9
4-Hydroxyisoleucine (4-Hydroxy-L-isoleucine) has antidepressant-like, antidyslipidemic, and antihyperglycemic effects. It displays an insulinotropic activity.
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L-Aspartic acid
Aspatofort, Asparagic acid
T2O273156-84-8
L-Aspartic acid (Aspatofort) is a non-essential amino acid in humans, L-Aspartic acid has an overall negative charge and plays an important role in the synthesis of other amino acids and in the citric acid and urea cycles. Asparagine, arginine, lysine, methionine, isoleucine, and some nucleotides are synthesized from aspartic acid. L-Aspartic acid also serves as a neurotransmitter.
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Methyl acetylacetate
Methyl acetoacetate
T4851105-45-3
Methyl acetylacetate (Methyl acetoacetate) has been identified in the urine of patients with an inherited deficiency of propionyl-CoA carboxylase, and after isoleucine loading in the diagnosis of 2-methylacetoacetyl-CoA thiolase deficiency.
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H-Abu-OH
L-α-amino-n-Butyric acid, L-Aminobutyric Acid, L(+)-2-Aminobutyric acid
T53061492-24-6
H-Abu-OH (L-α-amino-n-Butyric acid) , also known as (S)-2-aminobutanoic acid, homoalanine, 2-AABA, ethylglycine, or L-butyrine, is a member of the class of compounds known as L-alpha-amino acids. H-Abu-OH is a non-proteogenic amino acid that can be found in the human kidney, in liver tissues, and in most biofluids or excreta (e.g. feces, breast milk, urine, and blood). Within the cell, H-Abu-OH is primarily located in the cytoplasm. H-Abu-OH is biosynthesized by transaminating oxobutyrate, a metabolite in isoleucine biosynthesis. As a non-proteogenic amino acid, H-Abu-OH can be used by nonribosomal peptide synthases.
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Kirromycin
T38275
Kirromycin is an antibiotic originally isolated from Streptomyces and an inhibitor of protein biosynthesis. It inhibits isoleucine incorporation, polyphenylalanine synthesis, and growth of B. brevis. Kirromycin inhibits elongation factor Tu-dependent peptidyl transfer activity in E. coli.
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Methylmalonyl-CoA tetralithium
Methylmalonyl coenzyme tetralithium,Isosuccinyl coenzyme A tetralithium
TN7730104809-02-1
Methylmalonyl-CoA tetralithium, also known as Methylmalonyl coenzyme A, serves as a metabolic byproduct derived from the breakdown of valine, isoleucine, methionine, threonine, odd-chain fatty acids, and cholesterol. It is converted into succinyl-CoA through the enzymatic activity of methylmalonyl-CoA mutase (MCM) in the presence of the coenzyme vitamin B12 [1].
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