Propionibacterium shermanii

In anaerobic (or more correcdy, almost anaerobic or microaerophilic) bacteria such as Propionibacterium shermanii a fundamental difference occurs in that the cobalt atom is introduced at a much earlier stage, possibly to precorrin-2 or precorrin-3 A. 

Nocardia rugosa Propionibacterium arabinosum Propionibacteriumfreudenreichii Propionibacterium pentosaceum Propionibacterium peterssoni Propionibacterium shermanii Propionibacterium technicum Propionibacterium vannielli Protaminobacter ruber Pseudomonas denitrificans Bhi bium meliloti Bhodopseudomonas capsulata Bhodopseudomonas spheroides Strigomonas oncopelti Streptomyces aureofaciens Streptomyces griseus Streptomyces olivaceus... 

Cyanocobalamin (vitamin B12) Propionibacterium freudenreichii Propionibacterium shermanii Pseudomonas denitriTicans Treatment of pernicious anaemia... 

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. 

Table 9.1 Test data methylmalonyl-coenzyme A epimerase from Propionibacterium shermanii...

The similarity between the structures of the corrinoids and the porphyrins becomes evident from comparison of cobyrinic acid (75) (the simplest of the corronoids so far isolated) with uroporphyrinogen III (70). The possibility of a biosynthetic relationship between these structures was suggested by Shemin, who reported the incorporation of [14C]ALA into vitamin Bn and confirmed by the subsequent demonstration that PBG was also incorporated. The ubiquitous precursorial role of uroporphyrinogen III in heme, chlorophyll and corrinoid biosynthesis proposed by Porra (65BBA(107)176) was, however, not substantiated by experimental evidence until much later, when under carefully controlled conditions cells of Propionibacterium shermanii were shown to incorporate radioactivity from [14C]uroporphyrinogen III into vitamin Bn (72JA8269). 

The manufacturing process for Swiss cheese was developed in Emmen-thal, Switzerland, hence the name Emmentaler cheese (known as Swiss cheese in the United States). It is hard, pressed-curd cheese with an elastic body and a mild, nut-like, sweetish flavor. Swiss cheese is best known for the large holes or eyes that develop in the curd as the cheese ripens. S. thermophilus andL. bulgaricus or Lactobacillus helveticus are used for acid production, which aids in expelling whey from the curd, whereas Propionibacterium shermanii is largely responsible for the characteristic sweet flavor and eye formation. 

Cyanocobalamin (vitamin Bl2) Propionibacterium shermanii. Pseudomonas dentrificans Food and animal feed supplement... 

Acetobacter aceti Clostridium thermoaceticum Propionibacterium shermanii Aspergillus niger Yarrowia lipolytica... 

Zhang, S.T., Matsuoka, H., and Toda, K. 1993. Production and recovery of propionic and acetic acids in electrodialysis culture of Propionibacterium shermanii. J. Ferment. Bioeng. 75, 276-282. 

Nitrobacter Winogradsky Nitrosomonas europaea Propionibacterium shermanii... 

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. 

PolyP metabolism has been most studied in Propionibacterium shermanii. Konovalova and Vorob eva (1972) have examined the PolyP content in this bacterium. In this study, 70-80 % of the total PolyP was found in the fraction extracted by hot perchloric acid at all... 

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.

J. E. Clark (1990). Purification of polyphosphate glucokinase from Propionibacterium shermanii. In E. A. Dawes (Ed.), Novel Biodegradable Microbial Polymers, Kluwer Academic Publishers, Dordrecht, The Netherlands, pp. 213-221. 

J. E. Clark, H. Beegen and H. G. Wood (1986). Isolation of intact chains of polyphosphate from Propionibacterium shermanii grown on glucose or lactate. J. Bacteriol., 168,1212-1219. 

L. V. Konovalova and L. I. Vorob eva (1972). The effect of polymyxin M on the accumulation of lipids and polyphosphates by cells of Propionibacterium shermanii (in Russian). Dokl. Vyssh. Shkoly. Ser. Biol., 7, 101-115. 

C. A. Pepin and H. G. Wood (1986). Polyphosphate glucokinase from Propionibacterium shermanii kinetics and demonstration that the mechanism involves both processive and nonprocessive type reactions. J. Biol. Chem., 261, 4476 -480. 

N. F. B. Phillips, P. J. Horn and H. G. Wood (1993). The polyphosphate and ATP dependent glucokinase from Propionibacterium shermanii both activities are catalyzed by the same protein. 

Oterholm, A., Ordal, Z.J. Witter, L.D. 1970. Purification and properties of glycerol ester hydrolase (lipase) from Propionibacterium shermanii. Appl. Microbiol. 20, 16-22. 

Brennan, P.J., and Ballou, C.E., 1968, Phosphatidylmyoinositol monomannoside in Propionibacterium shermanii. Biochem. Biophys. Res. Commun. 30 69-75. 

Francalanci, F., Davis, N. K., Fuller, J. Q., Murfitt, D., and Leadlay, P. F., 1986, The subunit structure of methylmalonyl-CoA mutase from Propionibacterium shermanii. Biochem. J. 236 489n494. 

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 ... 

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