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Selenomonas ruminantium

Asanuma, N. Hino, T. Molecular characterization, enzyme properties and transcriptional regulation of phosphoenolpyruvate carboxykinase and pyruvate kinase in a ruminal bacterium, Selenomonas ruminantium. Microbiology, 147, 681-690 (2001)... [Pg.66]

Kamio, Y., Pdsa, H., Terawaki, Y., and Paulin, L. (1986). Cadaverine covalently linked to an essential constituent of the peptidoglycan necessary for the normal growth in Selenomonas ruminantium. J. Biol. Chem. 261, 6585-6589. [Pg.361]

Selenomonas ruminantium JCM 6582T Selenomonas ruminantium GA192T Propionispira arcuata WK011T 1 Propionispira arboris DSM 2179T... [Pg.196]

The bacteria number 10 -10 ° per millilitre of rumen contents. Over 200 species have been identified, and for descriptions of them the reader is referred to the works listed at the end of this chapter. Most of these bacteria are non-spore-forming anaerobes. Table 8.3 lists a number of the more important species and indicates the substrate they utilise and the products of the fermentation. This information is based on studies of isolated species in vitro and is not completely applicable in vivo. For example, it appears from Table 8.3 that succinic acid is an important end product, but in practice this is converted into propionic acid by other bacteria such as Selenomonas ruminantium (see Fig. 8.6) such interactions between microorganisms are an important feature of rumen fermentation. A further point is that the activities of a given species of bacteria may vary from one strain of that species to another. The total... [Pg.173]

Sivakumaran S, Molan AL, Meagher LP, Kolb B, Foo LY, Lane GA, Attwood GA, Fraser K, Tavendale M (2004) Variation in antimicrobial action of proanthocyanidins from Dorycnium rectum against rumen bacteria. Phytochemistry 65 2485-2497 Skene IK, Brooker JD (1995) Characterization of tannin acylhydrolase activity in the ruminal bacterium Selenomonas ruminantium. Anaerobe 1 321-327 Sly LI, Cahill MM, Osawa R, Fujisawa T (1997) The tannindegrading species Streptococcus gallolyticus and Streptococcus caprinus are subjective synonyms. Int J Syst Bacteriol 47 893-894... [Pg.261]

Selenomonas ruminantium, a Gram-negative anaerobe and one of the major species present in the rumen, accumulates succinate as a major end product in the presence of lactate, if malate is added to stimulate lactate uptake. Without malate present, the major end products are acetate and propionate. When succinate reached the concentration of the added malate, malate utilization ended. From a practical standpoint, malate could be added to ruminant diets high in rapidly fermentable carbohydrates. Because high rumen lactate is undesirable, the presence of malate could stimulate lactate utilization (Evans and Martin 1997). [Pg.48]

Keywords 22-kDa protein P22 Bacterial antizyme Cadaverine Lysine/ ornithine decarboxylase Ribosomal protein LIO Selenomonas ruminantium... [Pg.101]

Fig. 8.1 Model of cadaverine biosynthesis, its P22-mediated regulation, and its role in the cell wall-anchoring system in Selenomonas ruminantium. Refer to the text for details... Fig. 8.1 Model of cadaverine biosynthesis, its P22-mediated regulation, and its role in the cell wall-anchoring system in Selenomonas ruminantium. Refer to the text for details...
Selenomonas ruminantium LDC/ODC shows eukaryotic ODC-like properties with respects to both the primary sequence homology and the enzymatic characteristics, representing a phylogenetically intriguing feature. [Pg.108]

Kamio Y, Takahashi H (1980) Outer membrane proteins and cell surface structure of Selenomonas ruminantium. J Bacteriol 141 899-907... [Pg.109]

Kamio Y, Terawaki Y (1983) Purification and properties of Selenomonas ruminantium lysine decarboxylase. J Bacteriol 153 658-664... [Pg.109]

Kamio Y, Itoh Y, Terawaki Y (1981) Chemical structure of peptidoglycan in Selenomonas ruminantium-. cadaverine links covalently to the D-gJuteunic acid residue of peptidoglycan. J Bacteriol 146 49-53... [Pg.109]

Takatsuka Y, Tomita T, Kamio Y (1999b) Identification of the amino acid residues conferring substrate specificity upon Selenomonas ruminantium lysine decarboxylase. Biosci Biotechnol Biochem 63 1843-1846... [Pg.109]

Takatsuka Y, Yamaguchi Y, Ono M et al (2000) Gene cloning and molecular characterization of lysine decarboxylase from Selenomonas ruminantium delineate its evolutionary relationship to ornithine decarboxylase from eukaryotes. J Bacteriol 182 6732-6741 Yamaguchi Y, Takatsuka Y, Kamio Y (2002) Identification of a 22-kDa protein required for the degradation of Selenomonas ruminantium lysine decarboxylase by ATP-dependent protease. Biosci Biotechnol Biochem 66 1431-1434... [Pg.109]

Yamaguchi Y, Takatsuka Y, Matsufuji S et al (2006) Characterization of a counterpart to mammalian ornithine decarboxylase antizyme in prokaryotes. J Biol Chem 281 3995-4001 Yamaguchi Y, Takatsuka Y, Kamio Y (2008) Two segments in bacterial antizyme P22 are essential for binding and enhance degradation of lysine/ornithine decarboxylase in Selenomonas ruminantium. J Bacteriol 190 442 46... [Pg.109]


See other pages where Selenomonas ruminantium is mentioned: [Pg.106]    [Pg.224]    [Pg.200]    [Pg.45]    [Pg.78]    [Pg.245]    [Pg.333]    [Pg.358]    [Pg.177]    [Pg.69]    [Pg.101]    [Pg.102]    [Pg.102]    [Pg.109]   
See also in sourсe #XX -- [ Pg.172 ]

See also in sourсe #XX -- [ Pg.245 , Pg.250 , Pg.253 , Pg.292 , Pg.333 , Pg.358 ]




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