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Carrier protein A9 desaturases

Figure 13.25 Three-dimensional structures of diiron proteins. The iron-binding subunits of (a) haemery-thrin, (b) bacterioferritin, (c) rubryerythrin (the FeS centre is on the top), (d) ribonucleotide reductase R2 subunit, (e) stearoyl-acyl carrier protein A9 desaturase, (f) methane monooxygenase hydroxylase a-subunit. (From Nordlund and Eklund, 1995. Copyright 1995, with permission from Elsevier.)... Figure 13.25 Three-dimensional structures of diiron proteins. The iron-binding subunits of (a) haemery-thrin, (b) bacterioferritin, (c) rubryerythrin (the FeS centre is on the top), (d) ribonucleotide reductase R2 subunit, (e) stearoyl-acyl carrier protein A9 desaturase, (f) methane monooxygenase hydroxylase a-subunit. (From Nordlund and Eklund, 1995. Copyright 1995, with permission from Elsevier.)...
Figure 13.26 Dioxygen-utilizing carboxylate-bridged diiron centres (a) Oxidized (top) and reduced (bottom) MMOH (b) oxidized (top) and Mnn-reconstituted ToMOH (bottom) (c) oxidized (top) and reduced (bottom) RNR-R2 (d) oxidized (top) and reduced (bottom) rubryerythrin (e) reduced stearoyl-acyl carrier protein A9 desaturase (f) reduced bacterioferritin (g) methaemerythrin. Fel is on the left and Fe2 on the right. (Reprinted with permission from Sazinsky and Lippard, 2006. Copyright (2006) American Chemical Society.)... Figure 13.26 Dioxygen-utilizing carboxylate-bridged diiron centres (a) Oxidized (top) and reduced (bottom) MMOH (b) oxidized (top) and Mnn-reconstituted ToMOH (bottom) (c) oxidized (top) and reduced (bottom) RNR-R2 (d) oxidized (top) and reduced (bottom) rubryerythrin (e) reduced stearoyl-acyl carrier protein A9 desaturase (f) reduced bacterioferritin (g) methaemerythrin. Fel is on the left and Fe2 on the right. (Reprinted with permission from Sazinsky and Lippard, 2006. Copyright (2006) American Chemical Society.)...
Broadwater, J. A., Ai, J., Loehr, T. M., Sanders-Loehr, J., and Fox, B. G., 1998, Peroxodiferric intermediate of stearoyl-acyl carrier protein A9 desaturase oxidase reactivity during single turnover and implications for the mechanism of desaturation. Biochemistry 37 14664nl4471. [Pg.271]

Figure 16-20 (A) The active site of hemerythrin showing the two iron atoms (green) and their ligands which include the (X oxo bridge and two bridging car-boxylate groups. From Lukat et al.193 The active site is between four parallel helices as shown in Fig. 2-22. (B) Stereoscopic view of the backbone structure of a A9 stearoyl-acyl carrier protein desaturase which also contains a diiron center. Figure 16-20 (A) The active site of hemerythrin showing the two iron atoms (green) and their ligands which include the (X oxo bridge and two bridging car-boxylate groups. From Lukat et al.193 The active site is between four parallel helices as shown in Fig. 2-22. (B) Stereoscopic view of the backbone structure of a A9 stearoyl-acyl carrier protein desaturase which also contains a diiron center.
In green plants a soluble A9 stearoyl-acyl carrier protein desaturase uses 02 and NADH or NADPH to introduce a double bond into fatty acids. The structure of this protein (Fig. 16-20B,C) is related to those of methane oxygenase and ribonucleotide reductase.333347 Tire desaturase mechanism is discussed in Chapter 21. [Pg.863]

R = (P03) ) [36] (c) a,fi-dehydrogenation of fatty acids by soluble stearoyl-ACP A9-desaturase (A9D) (R = holo-acyl carrier protein) [37],... [Pg.39]


See other pages where Carrier protein A9 desaturases is mentioned: [Pg.236]    [Pg.238]    [Pg.276]    [Pg.619]    [Pg.236]    [Pg.238]    [Pg.276]    [Pg.619]    [Pg.127]    [Pg.391]   
See also in sourсe #XX -- [ Pg.236 ]




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