Valine
Isoleucine
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.
Amino Acids
Acetolactate Synthase
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
'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
Threonine
Amino Acids, Essential
Amino Acid Sequence
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.
Molecular Sequence Data
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.
Oxo-Acid-Lyases
Hydro-Lyases
Alanine
Mutation
Nutritional Requirements
Transaminases
Acremonium
Phenylalanine
Ketol-Acid Reductoisomerase
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.
Escherichia coli
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.
Isoleucine-tRNA Ligase
An enzyme that activates isoleucine with its specific transfer RNA. EC 6.1.1.5.
Isobutyrates
Decarboxylation
Mutagenesis, Site-Directed
Enzyme Repression
Carbon Isotopes
Amino Acid Substitution
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.
Base Sequence
Methylmalonate-Semialdehyde Dehydrogenase (Acylating)
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.
Norleucine
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.
Nitrogen
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.
Glycine
Nitrosoguanidines
Leucine Dehydrogenase
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+.