Propionibacterium shermanii, enzymes

Certain enzymes catalyze their reactions by way of a multisite mechanism in which the covalently linked intermediate is attached to a long arm that swings from one subsite to another subsite within the enzyme. In some cases, the covalently tethered intermediate can actually be transferred between subunits that form the active site. An example is Propionibacterium shermanii transcarboxylase an enzyme that catalyzes the biotin-dependent conversion of methylmalonyl-CoA and pyruvate to propionyl-CoA and oxaloacetate. Carboxylated biotin allows the two catalytic subsites to operate on the same reaction intermediate. 

The enzyme was partly purified from Propionibacterium shermanii (Robinson et al., 1987), and was shown to be a monomeric enzyme with a molecular mass of 83 kDa. It was demonstrated that short-chain PolyPs of 6-80 residues serve as primers for the synthesis of long-chain PolyPs using ATP by a strictly processive mechanism. The largest PolyPs synthesized was PolyP75o. 

Figure 8.12 Changes in polyphosphate and polyphosphate-metabolising enzymes during the development of a culture of Propionibacterium shermanii under normal conditions, and in the presence of polymyxin M (Kulaev et al., 1973a) (1) control conditions (2) polymyxin M (a) total PolyP (b) 1,3-diphosphoglycerate-polyphosphate phosphotransferase (c) polyphosphate kinase (d) polyphosphate-glucokinase (e) tripolyphosphatase (f) exopolyphosphatase with PolyP29o.

Several enzymes using PPj as phosphoryl donor have been described in bacteria and parasitic amoebae [22-24]. In both Propionibacterium shermanii and the eukaryote Entamoeba histolytica, the enzyme PPi-phosphofructose dikinase has been found [39,40]. This enzyme uses PPj as the phosphoryl donor to fructose-6-phosphate instead of ATP ... 

Meier B, Sehn AP, Michel C and Saran M (1994a) Reactions of hydrogen peroxide with superoxide dismutase from Propionibacterium shermanii - an enzyme which is equally active with iron or manganese - are independent of the prosthetic metal. Arch Biochem Biophys 313 296-303. 

The lipase/esterase of Pediococcus spp. has received little attention. Tza-netakis and Litopoulou-Tzanetaki (1989) found only weak esterase and lipase activities in a number of strains of P. pentosaceus of dairy origin by means of the API-ZYM system. Bhowmik and Marth (1989) found esterase activity in six strains of P. pentosaceus but none in two strains of P. acidilac-ticL The lipases of Propionibacterium shermanii studied by Oterholm et al. (1970) were optimally active at pH 7.2 and 47°C on tributyrin the enzymes showed a high preference for tripropionate and tributyrin and were inhibited by Hg and Na2HAs04 but not by pCMB or EDTA. Some esterase activity was observed but the enzyme was more active on emulsified than on soluble substrates. 

Kulaev IS, Vorobjeva LI, Konovalova LV, Bobik MA and Urison SO (1973) Enzymes of polyphosphate metabolism m Propionibacterium shermanii growing under normal conditions and in the presence of polymyxin M. Biokhimiya 38 595-599... 

Schwartz AC, Mertens B, Voss KW and Hahn H (1976) Inhibition of acetate and propionate formation upon aeration of resting cells of the anaerobic Propionibacterium shermanii evidence of the Pasteur reaction. Z Allg Mikrobiol 16 123-131 Scott AI (1994) Recent studies of enzymically controlled steps in vitamin B biosynthesis. 

The synthesis of methionine, the formation of methane, and the formation of acetate furnish examples of the capacity of Co-corrinoid compounds to act as carriers in methyl transfer reactions. At the present time it is difficult to judge whether this chemical capability of the Co-corrinoid compounds has been utilized more widely in nature for other transmethylation reactions. It has recently been reported that CHs-cobalamin can serve as a methyl donor in the formation of methylated bases in transfer RNA. Although a significant rate of nonenzymic reaction occurred, enzymes from both rat liver and the bacterium Propionibacterium shermanii increased die rate of methylation (Walerych et al., 1966). When extracts of a methane-forming bacterium were incubated with CHa-Bi2 and mer-... 

Transcarboxylase. Methylmalonyl-CoA transcarboxylase, which is induced in Propionibacterium shermanii, catalyzes the transcarboxylation between methylmalonyl-CoA and pyruvate (48). This ATP-independent enzyme is important in the metabolism of propionate. 

Ten strains of Propionibacterium shermanii have been tested for jS-D-galacto-sidase activity against 2-nitrophenyl jS-o-galactopyranoside the relation between the production of the enzyme and the stage of growth was examined. The enzyme was inhibited by blocking of its sulphydryl groups, but this inhibition was partly reversed with 1,4-dithiothreitol. 

P-D-Galactosidases.—A jS-o-galactosidase from Propionibacterium shermanii has been derivatized with thiol-blocking groups these modifications inhibited the enzymic activity, which was partly restored by the action of 1,4-dithiothreitol. ... 

Lin, T. Y., Lin, C. W., Wang, Y. J. (2002). Linoleic acid isomerase activity in enzyme extracts from Lactobacillus acidophilus and Propionibacterium ffeudenreichii ssp. shermanii. Journal of Food Science, 67,1502-1505. 

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