Information about Transamination
Transamination (or aminotransfer) is the reaction between an amino acid and an alpha-keto acid. The amino group is transferred from the former to the latter; this results in the amino acid being converted to the corresponding α-keto acid, while the reactant α-keto acid is converted to the corresponding amino acid (if the amino group is removed from an amino acid, an α-keto acid is left behind).
Transamination in biochemistry is accomplished by enzymes called transaminases or aminotransferases. The human body synthesizes the 10 non-essential amino acids and transamination is the process by which most of these syntheses occur. The chirality of an amino acid is determined during transamination. This reaction uses the coenzyme PLP, and is considered to be a kinetically perfect reaction. The product of transamination reactions depend on the availability of alpha-keto acids. The products usually are either alanine, aspartate or glutamate, since their corresponding alpha-keto acids are produced through metabolism of fuels.
Transamination in biochemistry is accomplished by enzymes called transaminases or aminotransferases. The human body synthesizes the 10 non-essential amino acids and transamination is the process by which most of these syntheses occur. The chirality of an amino acid is determined during transamination. This reaction uses the coenzyme PLP, and is considered to be a kinetically perfect reaction. The product of transamination reactions depend on the availability of alpha-keto acids. The products usually are either alanine, aspartate or glutamate, since their corresponding alpha-keto acids are produced through metabolism of fuels.
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amino acid is a molecule that contains both amine and carboxyl functional groups. In biochemistry, this term refers to alpha-amino acids with the general formula H2NCHRCOOH, where R is an organic substituent.
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A reactant or reagent is a substance consumed during a chemical reaction.[1] Solvents and catalysts, although they are involved in the reaction, are usually not referred to as reactants.
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Biochemistry is the study of the chemical processes in living organisms.[1] The word "biochemistry" comes from the Greek word βιοχημεία biochēmeia, which means "the chemistry of life.
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transaminase or an aminotransferase is an enzyme that catalyzes a type of reaction between an amino acid and an α-keto acid. Specifically, this reaction (transamination) involves removing the amino group from the amino acid, leaving behind an α-keto acid, and
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The term chiral (pronounced /ˈkaɪɹ(ə)l̩/) is used to describe an object that is non-superimposable on its mirror image. In terms of chemistry, such objects are usually molecules.
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Pyridoxal-phosphate (PLP, pyridoxal-5'-phosphate) is a coenzyme of many enzymatic reactions. It is the active form of vitamin B 6 which comprises three natural organic compounds, pyridoxal, pyridoxamine and pyridoxine.
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A catalytically perfect enzyme or kinetically perfect enzyme is an enzyme that catalyzes so efficiently, that almost every time enzyme meets its substrate, the reaction occurs.
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Alanine (abbreviated as Ala or A)[1] is an α-amino acid with the chemical formula HO2CCH(NH2)CH3. The L-isomer is one of the 20 proteinogenic amino acids, i.e. the building blocks of proteins.
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Aspartic acid or aspartate (abbreviated as Asp or D; Asx or B represent either aspartic acid or asparagine)[1] is an α-amino acid with the chemical formula HO2CCH(NH2)CH2CO2H.
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Glutamic acid or glutamate (abbreviated as Glu or E; Glx or Z represents either glutamic acid or glutamine), is the protonated form of glutamate (the anion). Glutamate is one of the 20 proteinogenic amino acids.
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transaminase or an aminotransferase is an enzyme that catalyzes a type of reaction between an amino acid and an α-keto acid. Specifically, this reaction (transamination) involves removing the amino group from the amino acid, leaving behind an α-keto acid, and
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