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L Ornithine

Manometric determiaation of L-lysiae, L-argioine, L-leuciae, L-ornithine, L-tyrosiae, L-histidine, L-glutamic acid, and L-aspartic acid has been reviewed (136). This method depends on the measurement of the carbon dioxide released by the T.-amino acid decarboxylase which is specific to each amino acid. [Pg.285]

L-Ornithine transcarbamoylase catalyzes transfer of the carbamoyl group of carbamoyl phosphate to ornithine, forming citrulline and orthophosphate (reaction 2, Figure 29-9). While the reaction occurs in the mitochondrial matrix, both the formation of ornithine and the subsequent metabolism of citmlline take place in the cytosol. Entry of ornithine into mitochondria... [Pg.246]

Figure 31-4. Conversion of spermidine to spermine. Spermidine formed from putrescine (decarboxylated L-ornithine) by transfer of a propylamine moiety from... Figure 31-4. Conversion of spermidine to spermine. Spermidine formed from putrescine (decarboxylated L-ornithine) by transfer of a propylamine moiety from...
Arginase 3.5.3.1 L-Arginine L-Ornithine/urea Urea-selective electrode... [Pg.288]

This enzyme [EC 1.5.1.24], also referred to as A -(1-l-carboxyethyl)-L-ornithine NADP+ oxidoreductase, reversibly catalyzes the reaction of ornithine with pyruvate and NADPH to produce A -(l-carboxyethyl)ornithine, NADP+, and water. Lysine can also serve as a substrate, acting on A , albeit not as effectively as ornithine. [Pg.112]

This enzyme [EC 2.3.1.35], also known as ornithine ace-tyltransferase, and ornithine transacetylase, catalyzes the reversible reaction of A -acetyl-L-ornithine with L-gluta-mate to produce L-ornithine and A-acetyl-L-glutamate. This protein also exhibits a low hydrolysis activity (about 1% of that of the transferase activity) of iV -acetyl-L-ornithine to yield acetate and L-ornithine. This enzyme is not identical with A-acetylglutamate synthase [EC 2.3.1.1]. [Pg.314]

This enzyme [EC 2.1.4.1], also known as L-arginine gly-cine amidinotransferase, catalyzes the reaction of L-argi-nine with glycine to produce L-ornithine and guanidi-noacetate. Canavanine can serve as the substrate instead of arginine. [Pg.320]

This enzyme [EC 1.5.1.19], also known as D-nopaline synthase, catalyzes the reaction of Al -(D-l,3-dicarboxy-propyl)-L-arginme with NADP+ and water to produce L-arginine, NADPH, and a-ketoglutarate (or, 2-oxoglu-tarate). In the reverse direction, the enzyme catalyzes the formation of D-nopaline from L-arginine as well as D-ornaline from L-ornithine. [Pg.509]

This enzyme [EC 1.5.1.11], also known as D-octopine synthase, catalyzes the reversible reaction of A -(d-1-carboxyethyl)-L-arginine with NAD+ and water to produce L-arginine, pyruvate, and NADH. The enzyme, in the reverse direction, will also act on L-ornithine, L-ly-sine, and L-histidine. [Pg.522]

This pyridoxal-phosphate-dependent enzyme [EC 4.1.1.17] catalyzes the conversion of L-ornithine to pu-trescine and carbon dioxide. [Pg.530]

Ferrichrome was the first siderophore to be isolated and characterized from the fungi Ustilago sphaerogena in 1952. It is a cyclic hexapeptide with the sequence cycto[(Gly)3-(Al -acetyl-Af -hydroxy-L-ornithine)3] (1) . The biologically active ferrichromes form iron(ni) complexes with a left-handed A-cis helical twist. [Pg.760]

Coprogen is a hnear trihydroxamate produced by Penicillium species and Neurospora crassa and was first isolated and characterized by Hesseltine and coworkers . Coprogens are predominantly produced by fungi species and frequently several coprogens are produced by the same species. Coprogen is composed of Af -acyl-A -hydroxy-L-ornithine, anhydromevalonic acid and acetic acid. [Pg.790]

True alkaloids derive from amino acid and they share a heterocyclic ring with nitrogen. These alkaloids are highly reactive substances with biological activity even in low doses. All true alkaloids have a bitter taste and appear as a white solid, with the exception of nicotine which has a brown liquid. True alkaloids form water-soluble salts. Moreover, most of them are well-defined crystalline substances which unite with acids to form salts. True alkaloids may occur in plants (1) in the free state, (2) as salts and (3) as N-oxides. These alkaloids occur in a limited number of species and families, and are those compounds in which decarboxylated amino acids are condensed with a non-nitrogenous structural moiety. The primary precursors of true alkaloids are such amino acids as L-ornithine, L-lysine, L-phenylalanine/L-tyrosine, L-tryptophan and L-histidine . Examples of true alkaloids include such biologically active alkaloids as cocaine, quinine, dopamine, morphine and usambarensine (Figure 4). A fuller list of examples appears in Table 1. [Pg.6]

True alkaloids L-ornithine Pyrrohdine alkaloids Pyrrohdine Cuscohygrine Hygrine... [Pg.7]

Figure 11. L-ornithine is an important precursor of pyrrolidine, tropane and pyrrolizidine alkaloids. Figure 11. L-ornithine is an important precursor of pyrrolidine, tropane and pyrrolizidine alkaloids.
Figure 15. L-ornithine and L-nicotinic acids are precursors of some aikaioids in the Nightshade famiiy. Figure 15. L-ornithine and L-nicotinic acids are precursors of some aikaioids in the Nightshade famiiy.
The Borage plant (syn. Forget-me-not) family (Boraginaceae Lindl.) contains L-ornithine (Figure 11 and 15) derived alkaloids, such as indicine-N-oxide in the heliotrope (Heliotropium indicum) and southern hound s tongue Cynoglosum creticum) species (Table 8). Farsam et al. reported on new alkaloids from... [Pg.28]


See other pages where L Ornithine is mentioned: [Pg.290]    [Pg.890]    [Pg.293]    [Pg.297]    [Pg.307]    [Pg.318]    [Pg.318]    [Pg.1116]    [Pg.1620]    [Pg.201]    [Pg.340]    [Pg.491]    [Pg.120]    [Pg.251]    [Pg.103]    [Pg.250]    [Pg.297]    [Pg.644]    [Pg.645]    [Pg.213]    [Pg.29]    [Pg.12]    [Pg.274]    [Pg.99]    [Pg.530]    [Pg.767]    [Pg.31]    [Pg.1]    [Pg.17]    [Pg.19]    [Pg.25]    [Pg.26]    [Pg.27]   
See also in sourсe #XX -- [ Pg.294 ]

See also in sourсe #XX -- [ Pg.444 ]

See also in sourсe #XX -- [ Pg.21 , Pg.284 , Pg.358 , Pg.366 , Pg.376 , Pg.472 , Pg.488 ]

See also in sourсe #XX -- [ Pg.6 ]




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