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Role of aspartate

Guengerich, F. P., Miller, G. P., Hanna, I. H., et al. (2002) Diversity in the oxidation of substrates by cytochrome P450 2D6 Lack of an obligatory role of aspartate 301-substrate electrostatic bonding. Biochemistry 41, 11,025-11,034. [Pg.512]

The role of aspartic acid and glutamic acid was investigated in BMP (Beefy Meaty peptide, Lys-Gly-Asp-Glu-Glu-Ser-Leu-Ala) isolated from enzymatic digests of beef soup. The taste of BMP was affected by the sequence of acidic fragment. Sodium ion uptake of acidic dipeptides and their taste, when mixed with sodium ion, were dependent on the component and/or sequence of dipeptides containing acicHc amino acids. [Pg.138]

Change of taste behavior of acidic peptides may cause various changes of the taste of mixture in which acidic peptides are contained. When we attempt to utilize the ionic taste, we must carefully think about the behavior of acidic peptides. These studies of taste of acidic peptide should give us useful information about the role of aspartic and glutamic in flavor enhancing and in designing taste of foods or sodium ion diet. [Pg.148]

K. Fallon, K. Bausch, J. Noonan, E. Huguenel, and P. Tamburini, Role of aspartic proteases in disseminated Candida albicans infection in mice, Infect. Immun., 65, 551, 1997. [Pg.116]

Hanna IH, Kim MS, Guengerich FP. Heterologous expression of cytochrome P450 2D6 mutants, electron transfer, and catalysis of bufuralol hydroxylation the role of aspartate 301 in structural integrity. Arch Biochem Biophys 2001 393 255-61. [Pg.460]

Fig. 5. Model for proton transfer in the bacterial reaction center of Rb. sphaeroides based on its known crystal structure. Some amino-acid residues are shown in the protein interior. See text for detaiis. Figure source Paddock, Rongey, McPherson, Juth, Feher and Okamura (1994) Pathway of proton transfer in bacterial reaction centers Role of aspartate-L213 in proton transfers associated with reduction of quinone to dihydroquinone. Biochemistry 33 743. Fig. 5. Model for proton transfer in the bacterial reaction center of Rb. sphaeroides based on its known crystal structure. Some amino-acid residues are shown in the protein interior. See text for detaiis. Figure source Paddock, Rongey, McPherson, Juth, Feher and Okamura (1994) Pathway of proton transfer in bacterial reaction centers Role of aspartate-L213 in proton transfers associated with reduction of quinone to dihydroquinone. Biochemistry 33 743.
Fig. 6. Photochemical cycles showing coupling of electron transfer to proton transfer, cytochrome oxidation and quinone exchange in (A) native reaction centers where two Cyt c are oxidized in the cycie, (B) reaction centers where uptake of the first proton is inhibited, and (C) reaction centers where uptake ofthe second proton is inhibited (shading indicates the quinone pool). Figure source (A) Paddock, Rongey, McPherson, Juth, Feher and Okamura (1994) Pathway of proton transfer in bacterial reaction centers role of aspartate-L21Z in proton transfers associated with reduction of quinone to dihydroquinone. Biochemistry 33 734 (B) Okamura and Feher (1992) Proton transfer in reaction centers from photosynthetic bacteria. Annu Rev Biochemistry. 61 868 (C) Feher, Paddock, Rongey and Okamura (1992) Proton transfer pathways in photosynthetic reaction centers studied by site-directed mutagenesis. In A Pullman, J Jortner and B Pullman (eds) Membrane Proteins Structures, Interactions and Models, p 485. Kluwer. Fig. 6. Photochemical cycles showing coupling of electron transfer to proton transfer, cytochrome oxidation and quinone exchange in (A) native reaction centers where two Cyt c are oxidized in the cycie, (B) reaction centers where uptake of the first proton is inhibited, and (C) reaction centers where uptake ofthe second proton is inhibited (shading indicates the quinone pool). Figure source (A) Paddock, Rongey, McPherson, Juth, Feher and Okamura (1994) Pathway of proton transfer in bacterial reaction centers role of aspartate-L21Z in proton transfers associated with reduction of quinone to dihydroquinone. Biochemistry 33 734 (B) Okamura and Feher (1992) Proton transfer in reaction centers from photosynthetic bacteria. Annu Rev Biochemistry. 61 868 (C) Feher, Paddock, Rongey and Okamura (1992) Proton transfer pathways in photosynthetic reaction centers studied by site-directed mutagenesis. In A Pullman, J Jortner and B Pullman (eds) Membrane Proteins Structures, Interactions and Models, p 485. Kluwer.
Collins, G.C.S. (1979) Evidence of a neurotransmitter role of aspartate and gamma-aminobutyric acid in the rat olfactory cortex. J. Physiol, 291, 51-60. [Pg.558]

Role of aspartate-279 in enhancing tiie function of PLP and in ALAS catalysis... [Pg.24]

Recall What is the metaholic role of aspartate transcarhamoylase ... [Pg.199]

Aspartate and norvaline have been reported to activate several plant threonine dehydratases (Kagan et al., 1969a Bleckman et al., 1971). Low concentrations of aspartate (1-5 mM) do not, however, affect the activity of the maize enzyme under any of a number of assay conditions that have been tested (E. Lissik and J. Bryan, unpublished). Although a role of aspartate as a feedforward pathway activator would be interesting, it has not been established that this amino acid is an important effector of any plant threonine dehydratase in vivo. [Pg.433]

Fitzpatrick S M, Cooper A J L, and Duffy T. E. (1983) Use of (3-methylene-D,L-aspartate to assess the role of aspartate aminotransferase in cerebral oxidative metabolism. / Neurochetn. 41, 1370-1383. [Pg.229]

E, E, Howell, J, E, Villafranca, M. S, Warren, S, J, Oatley, and J. Kraut, Science, 231,1123 (1986), Functional Role of Aspartic Acid-27 in Dihydrofolate Reductase Revealed by Mutagenesis,... [Pg.300]

FIG u R E 9.1 2 The role of aspartate as a nitrogen donor in synthetic reactions, and of adenosine deaminase as a source of ammonium ions. [Pg.273]

Citrulline, a non-protein amino acid, was identified independently by Mitsimori Wada in watermelon juice (Wada, 1930) and by Dankwart Ackermann as a product of the degradation of arginine (Ackermann, 1931). Soon afterwards, Hans Krebs and Kurt Henseleit (Krebs and Henseleit, 1932) proposed the first metabolic cycle ever described, in which citrulline was an intermediary in the synthesis of urea. A few years later, the role of aspartate as the donor of the second nitrogen for urea synthesis was established by Sarah Ratner (Ratner and Pappas, 1949). [Pg.87]


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