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Thermoplasma acidophilum

Neutral gangliolipids from Thermoplasma acidophilum were separated by PTLC, and their tentative structures were characterized by the combination of GC, H-NMR, and FAB-mass spectrometries [91]. The lipophilic portion of the neutral glycolipid was composed of caldarchaeol (dibiphytanyl-diglycerol tetraether), and the sugar moieties of the glycolipids were composed of glucose. [Pg.321]

Kurz LC, Fite B, Jean J, Park J, Erpelding T, Callis P (2005) Photophysics of tryptophan fluorescence link with the catalytic strategy of the citrate synthase from Thermoplasma acidophilum. Biochemistry 44(5) 1394-1413... [Pg.327]

E. Seemiiller, A. Lupas, D. Stock, J. Lowe, R. Huber, W. Baumeister, Proteasome from Thermoplasma Acidophilum A Threonine Protease , Science 1995, 268, 579-582. [Pg.59]

Navigation inside a protease substrate selection and product exit in the tricorn protease from Thermoplasma acidophilum. [Pg.283]

Akopian, T. N., Kisselev, A. F., and Goldberg, A. L. Processive degradation of proteins and other catatlytic properties of the proteasome from Thermoplasma acidophilum. J. Biol. [Pg.313]

An example of a whole-cell process is the two-step synthesis of an enantiopure epoxide by asymmetric reduction of an a-chloro ketone (Scheme 6.4), catalyzed by recombinant whole cells of an Escherichia coli sp. overexpressing an (R)-KRED from Lactobacillus kefir and GDH from Thermoplasma acidophilum, to the corresponding chlorohydrin, followed by non-enzymatic base-catalyzed ring closure to the epoxide [17]. [Pg.114]

S proteasomes are ubiquitous and essential in eukaryotes (Heinemeyer 2000) ubiquitous but not essential in archaea (Ruepp et al. 1998) and rare and non-essential in bacteria (Knipfer and Shrader 1997 Ete Mot et al. 1999). Because of ist relative simplicity the proteasome from the archaeon Thermoplasma acidophilum (Dahlmann et al. 1989) has played a pivotal role in resolving the structure and enzymatic mechanism of 20S proteasomes (see for example Hegerl et al. 1991 Grziwa et al. 1991 Piihler et al. 1992 Zwickl et al. 1992 Jap et al. 1993). [Pg.68]

The structure of the 20S proteasome (fig. 2.16) from Thermoplasma acidophilum displays four rings stacked upon each other surroimding a central cavity in which pro-... [Pg.111]

Since cinnamyl aldehyde is the main component of cassia oil (approximately 90%) and Sri Lanka cinnamon bark oil (approximately 75%) [49], it is industrially more important to generate cinnamyl alcohol, which is less abundantly available from nature but is important as cinnamon flavour, by biotransformation of natural cinnamyl aldehyde than vice versa. Recently, a whole-cell reduction of cinnamyl aldehyde with a conversion yield of 98% at very high precursor concentrations of up to 166 g L was described [136]. Escherichia coli DSM 14459 expressing a NADPH-dependent R alcohol dehydrogenase from Lactobacillus kefir and a glucose dehydrogenase from Thermoplasma acidophilum for intracellular cofactor regeneration was applied as the biocatalyst (Scheme 23.8). [Pg.539]

While chaperonins assist proteins to fold correctly proteasomes destroy unfolded chains by partial hydrolysis, cutting the chains into a random assortment of pieces from 3 to 30 residues in length with an average length of 8 residues/ Proteasomes destroy not only unfolded and improperly folded proteins but also proteins marked for destruction by the ubiquitin system described in Box 10-C. It has been hard to locate true proteosomes in most bacteria. However, they do contain protease particles with similar characteristics2-1 and archaeons, such as Thermoplasma acidophilum, have proteasomes similar to those of eukaryotes.cc... [Pg.340]

V-ATPase A-ATPasea Thermoplasma acidophilum F-ATPase Escherichia coli... [Pg.347]

AThe subunit has been confirmed for the insect (Merzendorfer et al, 1999) and chromaffin granule enzyme (Ludwig et al, 1998) and has recently been found in the yeast enzyme (Sambade and Kane, 2004). The subunit compositions of the F-ATPase from the bacterium Escherichia coli, the vacuolar ATPase from yeast and bovine brain clathrin-coated vesicles, and the A-ATPase from the Archaeon Thermoplasma acidophilum are listed. Molecular masses are calculated from the amino acid sequence where available. [Pg.347]

Fig. 1. Working models of the F-, V-, and A-ATPases. Model of the subunit arrange-mentin the (A) FjFo-ATP synthase from Escherichia colt, (B) vacuolar ATPase from bovine brain clathrin- coated vesicles, and (C) A A0-ATPase from Thermoplasma acidophilum. The catalytic domain is in blue, the rotor domain is in green, and the stator domain is in orange. Fig. 1. Working models of the F-, V-, and A-ATPases. Model of the subunit arrange-mentin the (A) FjFo-ATP synthase from Escherichia colt, (B) vacuolar ATPase from bovine brain clathrin- coated vesicles, and (C) A A0-ATPase from Thermoplasma acidophilum. The catalytic domain is in blue, the rotor domain is in green, and the stator domain is in orange.
Thermoplasma acidophilum Acidophile Label-free Metabolic pathway analysis (220)... [Pg.189]

Fig. 3. Pathways of glucose catabolism in halophilic and thermophilic archaebacteria. The modified Entner-Doudoroff pathway of halophiles (solid lines) and the non-phosphorylated Entner-Doudoroff pathway of Sulfolobus sol/ataricus and Thermoplasma acidophilum (dashed lines) are shown in comparison with the classical Entner-Doudoroff pathway of eubacteria (heavy solid lines) from Fig. 1. Fig. 3. Pathways of glucose catabolism in halophilic and thermophilic archaebacteria. The modified Entner-Doudoroff pathway of halophiles (solid lines) and the non-phosphorylated Entner-Doudoroff pathway of Sulfolobus sol/ataricus and Thermoplasma acidophilum (dashed lines) are shown in comparison with the classical Entner-Doudoroff pathway of eubacteria (heavy solid lines) from Fig. 1.
Thermoplasma acidophilum and Thermoplasma volcanium are facultative organo-trophs [47], and are phylogenetically related to the halophiles. When growing aerobically. [Pg.9]

Fig. 22. Glycan structures of cytoplasmic membrane components of Thermoplasma acidophilum (a) glycoprotein (parentheses indicate variable numbers K... Fig. 22. Glycan structures of cytoplasmic membrane components of Thermoplasma acidophilum (a) glycoprotein (parentheses indicate variable numbers K...
Thermoplasma acidophilum, a wall-less mycoplasma-like aerobe, is the one species of Thermoplasma that has been examined for lipids [9]. Its polar lipids contain at least six different glycolipids and at least seven phosphorus-containing lipids, all based on... [Pg.274]


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See also in sourсe #XX -- [ Pg.1155 ]

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Thermoplasma acidophilum proteasome

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