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Oxalate decarboxylase

Copper is a component of the oxalate decarboxylase in Bacillus subtilis that converts oxalate into formate and CO2 (Tanner et al. 2001). [Pg.185]

Tanner A, L Bowater, SA Fairhurst, S Bornemann (2001) Oxalate decarboxylase requires manganese and dioxygen for activity. J Biol Chem lib 43627-43634. [Pg.192]

Tanner A, S Bornemann (2000) Bacillius subtilis YvrK is an acid-induced oxalate decarboxylase. J Bacteriol 182 5271-5273. [Pg.335]

Azam, M., Kesarwani, M., Natarajan, K. and Datta, A. (2001) A secretion signal is present in the Collybia velutipes oxalate decarboxylase gene. Biochemical and Biophysical Research Communications, 289 (4), 807-812. [Pg.56]

Dashek WV, Micales JM. Purification of enzymes oxalate decarboxylase, in Methods in Plant Biochemistry and Molecular Biology (Dashek WV, ed.), CRC Press, Boca Raton, FL, 1997, pp. 49-71. [Pg.179]

Triton X-100-Promoted Solubilization o/Postia Placenta Hyphal Sheath Oxalate Decarboxylase... [Pg.187]

Micales JA. Oxalate decarboxylase in the brown-rot wood decay fungus, Postia placenta. Mat U Org 1995 29 177. [Pg.194]

Lahrou NE, Clonis YD. Biomimetic dye-ligand for oxalate requiring enzymes Studies with oxalate oxidase and oxalate decarboxylase. J Biochem 1995 40 59. [Pg.195]

Figure 27 Schematic of one active site of oxalate decarboxylase from Bacillus subtilis. The other active site is similar but a water molecule replaces the formate. Figure 27 Schematic of one active site of oxalate decarboxylase from Bacillus subtilis. The other active site is similar but a water molecule replaces the formate.
Oxalate is determined by using either oxalate decarboxylase (246-248) or oxalate oxidase (242,249) immobilized electrodes. In the former, the CO2 liberated and detected is proportional to the logarithm of the oxalate concentration. Linearity is reported from 0.2 to 10 mM, and the electrodes are stable for more than one month. Human control samples, spiked with oxalate, have been analyzed (246). Oxalate oxidase can be immobilized onto an O2 electrode (242), an amperometric H2O2 sensor (246, 249, 250), and a potentiometric CO2 probe (246) ... [Pg.96]

Although white-rot fungi also secrete H2O2 (104), they have not been found to depolymerize cellulose oxidatively. One reason might be that they possess oxalate decarboxylase, which decomposes oxalate, whereas brown-rot fungi apparently do not (98). This problem deserves further investigation. [Pg.476]

L-lactate and oxalate were also tested with lactate-2-monoxygenase and oxalate decarboxylase and excellent results were obtained. CPG columns were employed in both instances. Good linearity was obtained between 0.005 -1 mM for L-lac-tate [3] and between 0.1-3 mM for oxalate [24]. Similarly, urea was measured with a precision better than 1 % in the linearity range 0.01-200 mM using Jack bean urease. The reaction of urea with ethanol to produce ethylcarbamate is of interest in fermentation monitoring. [Pg.25]

The determination of oxalate in urine is required for diagnosis of renal calculus and hyperoxaluria. For enzymatic oxalate determination, oxalate decarboxylase (EC 4.1.1.2) has been employed in enzyme thermistors (Danielsson etal., 1981), enzyme reactors (Lindberg, 1983), and potentiometric enzyme electrodes (Kobos and Ramsey, 1980). [Pg.153]


See other pages where Oxalate decarboxylase is mentioned: [Pg.486]    [Pg.256]    [Pg.317]    [Pg.9]    [Pg.33]    [Pg.185]    [Pg.187]    [Pg.96]    [Pg.96]    [Pg.97]    [Pg.138]    [Pg.2556]    [Pg.646]    [Pg.145]    [Pg.41]    [Pg.294]    [Pg.99]    [Pg.2555]    [Pg.259]    [Pg.368]    [Pg.369]    [Pg.369]    [Pg.66]    [Pg.239]   
See also in sourсe #XX -- [ Pg.185 ]

See also in sourсe #XX -- [ Pg.368 ]

See also in sourсe #XX -- [ Pg.66 ]




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Enzyme oxalate decarboxylase

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