Purification and subunit determination of the nickel-dependent Staphylococcus xylosus urease

Christians, S

doi:10.1016/0378-1097(91)90608-d

Cited by 5 publications

(8 citation statements)

References 7 publications

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“…As detailed above, urease sequences make up a highly related family of proteins; hence, it is likely that all ureases contain a metallocenter containing two nickel ions. It must be pointed out, however, that selected microorganisms (e.g., Arthrobacter oxydans [256], B. pasteurii [34], Brevibacterium ammoniagenes [219], H. pylori [109,291], S. xylosus [33], and S. saprophyticus [255]) are reported to have lower nickel contents that, in some cases, are near those expected for proteins possessing a mononickel center. Although it is possible that ureases fall into two classes with distinct nickel-containing active sites, it seems more likely that the anomalous low levels of nickel in these isolated examples arise from incomplete loading of the protein with the metal ion.…”

Section: Active-site Studies Of Ureasementioning

confidence: 98%

“…xylosus [33], S. saprophyticus [255], M. morganii [118], and several other species [201] are larger). In particular, the H. pylori enzyme consistently has been reported to be significantly larger, with an M r of 380,000 to 600,000 (72,78,116,291).…”

Section: General Protein Structure Of Ureasesmentioning

confidence: 99%

“…In contrast, as previously pointed out (201), other purified bacterial ureases generally possess specific activities of 1,000 to 5,500 U/mg. Recently published examples of this trend include the isolated H. pylori, M. morganii, Helicobacter mustelae, S. xylosus, and S. saprophyticus ureases, which possess specific activities of 1,100 to 3,189 U/mg (72,78,116), 2,130 U/mg (118), 1,560 U/mg (73), 1,573 U/mg (33), and 1,979 U/mg (255), respectively, whereas a slightly higher value of 9,300 U/mg is reported for the Sporosarcina ureae enzyme (184). Ureases from two filamentous cyanobacteria have recently been purified and found to possess specific activities of 200 to 350 U/mg (124).…”

Section: Urease Enzymologymentioning

confidence: 99%

See 2 more Smart Citations

Molecular biology of microbial ureases.

Mobley

Island

Hausinger

1995

Microbiological Reviews

873

572

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Section: Active-site Studies Of Ureasementioning

confidence: 98%

Section: General Protein Structure Of Ureasesmentioning

confidence: 99%

Section: Urease Enzymologymentioning

confidence: 99%

See 1 more Smart Citation

Molecular biology of microbial ureases.

Mobley

Island

Hausinger

1995

Microbiological Reviews

873

572

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“…Halotolerant ureaseproducing bacteria (UPB) are mainly the Gram-positive species of Sporosarcina pasteurii (former Bacillus pasteurii) and physiologically similar species of the genus Bacillus: B. cereus (Castanier et al 2000), B. megaterium Dhami et al 2014), B. sphaericus (De Muynck et al 2011;Hammes et al 2003Hammes et al , 2008aWang et al 2012 (Sarda et al 2009), Bacillus sp. (Hammes et al 2003;Lisdiyanti et al 2011;Stabnikov et al 2011Stabnikov et al , 2013a, or halotolerant species from genus Staphylococcus (Christians et al 1991;Jin et al 1994Jin et al , 2004Stabnikov et al 2013a, b). It could be expected that the extreme halophiles Haloarcula aidinensis, H. hispanica, H. japonica, and H. marismortui that show maximum urease activity at 18-23 % NaCl (Mizuki et al 2004) could be also used.…”

Section: First Type Of Calcium-based Biocementation/ Biogroutingmentioning

confidence: 95%

Construction Biotechnology: a new area of biotechnological research and applications

Stabnikov

Ivanov

Chu

2015

World J Microbiol Biotechnol

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A new scientific and engineering discipline, Construction Biotechnology, is developing exponentially during the last decade. The major directions of this discipline are selection of microorganisms and development of the microbially-mediated construction processes and biotechnologies for the production of construction biomaterials. The products of construction biotechnologies are low cost, sustainable, and environmentally friendly microbial biocements and biogrouts for the construction ground improvement. The microbial polysaccharides are used as admixtures for cement. Microbially produced biodegradable bioplastics can be used for the temporarily constructions. The bioagents that are used in construction biotechnologies are either pure or enrichment cultures of microorganisms or activated indigenous microorganisms of soil. The applications of microorganisms in the construction processes are bioaggregation, biocementation, bioclogging, and biodesaturation of soil. The biotechnologically produced construction materials and the microbially-mediated construction technologies have a lot of advantages in comparison with the conventional construction materials and processes. Proper practical implementations of construction biotechnologies could give significant economic and environmental benefits.

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“…The ureases of Helicobacter species are composed of two subunits of approximately 26.5 (UreA) and 60.3 (UreB) kDa. The ureases of non-Helicobacter bacterial species have three subunits of 6 to 14 kDa (UreA), 11 to 20 kDa (UreB), and 60 to 70 kDa (UreC) (2,4,5,7,15,20,23,25,33,41). The amino acid sequence of the large UreC subunit of the non-Helicobacter bacterial species is homologous to that of the large UreB subunit of Helicobacter species.…”

mentioning

confidence: 99%

Urease from a potentially pathogenic coccoid isolate: purification, characterization, and comparison to other microbial ureases

Lee

Calhoun

1997

Infect Immun

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Strain SL100 is a gram-positive coccoid isolate prototype with an adhesin specific for gastric mucin and is representative of potentially pathogenic organisms obtained at biopsy from patients with gastric disorders. The urease of this isolate constitutes a significant fraction of the total cell protein, and the outcome of the purification strategy described herein suggests that it is associated with a cell wall fraction. The urease was purified 138-fold to apparent homogeneity, as indicated by gel electrophoresis, to a specific activity of 1,120 U/mg. The urease was unstable during purification in the absence of nickel, which is present in a metallocenter in other microbial ureases. When nickel sulfate was present during growth (5 M) and in buffers during sonication and purification (100 M), the urease was completely stable at room temperature during the purification procedure. The native urease was approximately 260 kDa and was composed of three subunits of 65 kDa and three subunits of 21 kDa. The purified urease was relatively stable in acid and retained most of its activity after incubation for 30 min at pH 1.3. The K m s for urease measured from whole cells and for the purified enzyme were 0.56 and 1.7 mM, respectively, indicating that some cell wall component(s) affects the affinity of the enzyme for urea. The V max s for urea hydrolysis measured from whole cells and for the purified enzyme were 8.1 and 1,120 mol/min/mg of protein, respectively. The kinetic parameters, relative abundance, and subunit composition are more similar to those of the ureases of Helicobacter than to those of the ureases of other microbial species. These similarities are consistent with an adaptation of this organism to colonization of the stomach and indicate that the urease may be a virulence factor during colonization.

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Purification and subunit determination of the nickel-dependent Staphylococcus xylosus urease

Cited by 5 publications

References 7 publications

Molecular biology of microbial ureases.

Molecular biology of microbial ureases.

Construction Biotechnology: a new area of biotechnological research and applications

Urease from a potentially pathogenic coccoid isolate: purification, characterization, and comparison to other microbial ureases

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