By Alton Meister (Auth.)
Biochemistry of the amino acids
summary: Biochemistry of the amino acids
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Even supposing much less universal than α-amino acids, non-α-amino acids—where the amino workforce isn't really at the carbon instantly adjoining to the carboxyl staff yet is hooked up to a different carbon within the chain (for instance, the β, γ, δ carbon)—are elements of biologically very important molecules, are major within the pharmaceutical undefined, and are worthy beginning fabrics for plenty of parts of natural chemistry.
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Additional info for Biochemistry of the Amino Acids
The rapid incorporation of labeled C 0 2 into glycolic acid and glycine during photosynthesis suggests conversion of glyoxylate to glycine (353-356). Another possible pathway of glyoxylate formation is deamination of aminoethanol to glycolaldehyde, and oxidation of the latter to glyoxylate (357, 358). Glycine is a product of the anaerobic degradation of purines by Clostridium cylindrosporum and C. acidiurici (359, 360). Rabinowitz and collaborators obtained evidence for the following pathway of xanthine degradation in these organisms: HO o H HN^y" I \^° || N > CH H Xanthine HO W H2N \ I 0 H I \ CH Mn++ > H 4-Ureido-5-imidazolecarboxylic acid O \ H || H CH 4-Amino-5-imidazolecarboxylic acid ► I CH H2N^ 4-Aminoimidazole > 638 VI.
After treatment with heat, urea, or heavy metal ions, the enzyme can no longer be D . Aspartic Acid and Asparagine 615 inhibited by cytidine 5'-triphosphate; such treatment increases activity and alters the K m for aspartate and the pH optimum. An enzyme that catalyzes the degradation of carbamyl aspartate to carbon dioxide, ammonia, and L-aspartate (ureidosuccinase) has been obtained from Zymobacterium oroticum (136). This reaction is analogous to that catalyzed by urease, and is essentially irreversible.
The most active of the excitatory amino acids examined were glutamic acid, ß-aminoglutaric acid, aspartic acid, cysteic acid, and cysteinesulfinic acid (292). A report has appeared describing the oxidation of y-aminobutyric acid to ß-hydroxy-y-aminobutyric acid by homogenates of rabbit and guinea pig brain. Oxygen utilization was observed and paper Chromatographie studies suggested formation of ß-hydroxy-y-aminobutyric acid (294). Studies on Clostridium aminobutyricum, which can utilize y-aminobutyric acid as its major sources of carbon, nitrogen, and energy, indicate that the degradation of y-aminobutyrate involves a coupling of the following reactions (295): 2 y-Aminobutyrate + 2 acetyl-coenzyme A -> 2 N H 3 + 2 crotonyl-coenzyme A + 2 acetate Crotonyl-coenzyme A + D P N H + H + -> butyryl-coenzyme A + D P N + Crotonyl-coenzyme A + D P N + + coenzyme A + H 2 0 -> 2 acetyl-coenzyme A + D P N H + H + 2 y-Aminobutyrate + H2O + coenzyme A -»■ 2 N H 3 + butyryl-coenzyme A + 2 acetate The last equation, which is the sum of the others, indicates that the degradation of 2 moles of y-aminobutyric acid leads to formation of one mole of a high-energy compound.
Biochemistry of the Amino Acids by Alton Meister (Auth.)