Pseudomonas molecular properties

Kuronen, T., and Ellfolk, N. (1972). A new purification procedure and molecular properties of Pseudomonas cytochrome oxidase. Biochim. Biophys. Acta 275, 308-318. 

Pseudomonas aeruginosa nitrite reductase of, 274, 275 transhydrogenase of, 53 molecular properties, 57 purification, 54, 56... 

Another source of rubredoxins was found in an aerobic bacterium, Pseudomonas oleovorans, utilizing n-hexane as a carbon source (10). This particular rubredoxin differs from those commonly found in anaerobic bacteria in some of its properties it has a molecular weight of 19,000, and one iron form of the protein is readily converted to a two-iron form (11). The rubredoxin of P. oleovorans functions as a terminal electron transfer component in an enzyme system which participates in the ( -hydroxylation of fatty acids and hydrocarbons. The hydrocarbon-oxidizing... 

Gilbert, E.J. (1993) Pseudomonas lipases biochemical properties and molecular cloning. Enz. Microb. Technol., 15, 634-645. 

During the period of time when the nature of the 19-nortestosterone acetate-dependent photoinactivation was under investigation, a new bacterial steroid isomerase was obtained from extracts of Pseudomonas putida (Biotype B) in nearly homogeneous form and some of its physical and enzymatic properties were characterized (64, 65, 66). The putida isomerase is similar in its molecular weight and quaternary structure to the testosteroni isomerase. Chemically, the most striking difference between the two isomerases is the presence of four residues of cysteine per polypeptide chain of the putida isomerase whereas no cysteine or cystine is present in the testosteroni isomerase. N-Terminal sequence analysis of the putida isomerase demonstrated substantial sequence homology between the two enzymes. 

Alanine racemases are homodimeric enzymes of an apparent molecular mass of 76kDa, containing two molecules of PLP as co-enzyme [61] the known enzymes from different sources are highly homologous. With regard to the kinetic properties, the values for D- and L-Ala determined at 30 °C for the Pseudomonas fiuorescens alanine racemase are -12 and 19mM, respectively and the Vnm values for racemization are -1200 and 2200 units/mg protein, respectively. The thermophilic alanine racemase from B. stearothermophilus is quite stable to heat treatment (up to 75 °C for 1 h) while the mesophilic one from B. subtilis is stable up to 55 °C under the same conditions. 

A number of reports have also dealt with the varied properties of pseudomonas R factors, such as their similarities and differences to F factors and other R factors [228] and with their molecular structure [230, 231]. 

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