A branched-chain essential amino acid that has stimulant activity. It promotes muscle growth and tissue repair. It is a precursor in the penicillin biosynthetic pathway.
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.
An essential branched-chain amino acid important for hemoglobin formation.
Amino acids which have a branched carbon chain.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
A flavoprotein enzyme that catalyzes the formation of acetolactate from 2 moles of PYRUVATE in the biosynthesis of VALINE and the formation of acetohydroxybutyrate from pyruvate and alpha-ketobutyrate in the biosynthesis of ISOLEUCINE. This enzyme was formerly listed as EC 4.1.3.18.
'Keto acids', also known as ketone bodies, are water-soluble compounds - acetoacetic acid, beta-hydroxybutyric acid, and acetone - that are produced during fat metabolism when liver glycogen stores are depleted, providing an alternative energy source for the brain and other organs in states of carbohydrate restriction or intense physical exertion.
Valerates are salts or esters formed from the reaction between valerianic acid and a base, characterized by their tranquilizing and sedative properties, often used in pharmaceuticals and dietary supplements for promoting sleep and reducing anxiety.
An essential amino acid occurring naturally in the L-form, which is the active form. It is found in eggs, milk, gelatin, and other proteins.
Amino acids that are not synthesized by the human body in amounts sufficient to carry out physiological functions. They are obtained from dietary foodstuffs.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Enzymes that catalyze the cleavage of a carbon-carbon bond of a 3-hydroxy acid. (Dorland, 28th ed) EC 4.1.3.
Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1.
A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
A sulfur-containing essential L-amino acid that is important in many body functions.
The amounts of various substances in food needed by an organism to sustain healthy life.
A subclass of enzymes of the transferase class that catalyze the transfer of an amino group from a donor (generally an amino acid) to an acceptor (generally a 2-keto acid). Most of these enzymes are pyridoxyl phosphate proteins. (Dorland, 28th ed) EC 2.6.1.
An enzyme that activates valine with its specific transfer RNA. EC 6.1.1.9
A mitosporic fungal genus with many reported ascomycetous teleomorphs. Cephalosporin antibiotics are derived from this genus.
An essential aromatic amino acid that is a precursor of MELANIN; DOPAMINE; noradrenalin (NOREPINEPHRINE), and THYROXINE.
The rate dynamics in chemical or physical systems.
An enzyme that catalyzes the oxidation of (R)-2,3-dihydroxy-3-methylbutanoate to (S)-2-hydroxy-2-methyl-3-oxobutanoate in the presence of NADP. It is involved in the biosynthesis of VALINE; LEUCINE; ISOLEUCINE; pentothenate and COENZYME A. This enzyme was formerly classified as EC 1.1.1.89.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
An enzyme that activates isoleucine with its specific transfer RNA. EC 6.1.1.5.
Aliphatic acids that contain four carbons in a branched-chain configuration. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the 2-carboxypropane structure.
The removal of a carboxyl group, usually in the form of carbon dioxide, from a chemical compound.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
The interference in synthesis of an enzyme due to the elevated level of an effector substance, usually a metabolite, whose presence would cause depression of the gene responsible for enzyme synthesis.
Stable carbon atoms that have the same atomic number as the element carbon, but differ in atomic weight. C-13 is a stable carbon isotope.
The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
An enzyme that plays a role in the VALINE; LEUCINE; and ISOLEUCINE catabolic pathways by catalyzing the oxidation of 2-methyl-3-oxopropanate to propanoyl-CoA using NAD+ as a coenzyme. Methylmalonate semialdehyde dehydrogenase deficiency is characterized by elevated BETA-ALANINE and 3-hydropropionic acid.
An essential amino acid. It is often added to animal feed.
An unnatural amino acid that is used experimentally to study protein structure and function. It is structurally similar to METHIONINE, however it does not contain SULFUR.
An element with the atomic symbol N, atomic number 7, and atomic weight [14.00643; 14.00728]. Nitrogen exists as a diatomic gas and makes up about 78% of the earth's atmosphere by volume. It is a constituent of proteins and nucleic acids and found in all living cells.
A non-essential amino acid. It is found primarily in gelatin and silk fibroin and used therapeutically as a nutrient. It is also a fast inhibitory neurotransmitter.
Nitrosoguanidines are organic compounds containing a nitroso group (-NO) and a guanidine group (-R1R2N-CN-), known for their alkylating properties and potential use as therapeutic agents or carcinogenic substances, depending on the specific compound and context.
Isomeric forms and derivatives of pentanol (C5H11OH).
An octameric enzyme belonging to the superfamily of amino acid dehydrogenases. Leucine dehydrogenase catalyzes the reversible oxidative deamination of L-LEUCINE, to 4-methyl-2-oxopentanoate (2-ketoisocaproate) and AMMONIA, with the corresponding reduction of the cofactor NAD+.