Urea amidolyase. I. Properties of the enzyme from Candida utilis.

نویسندگان

  • R J Roon
  • B Levenberg
چکیده

Candida utilis contains an inducible enzyme, urea amidolyase, which catalyzes the decomposition of urea with formation of carbon dioxide and ammonia. This reaction is accompanied by the cleavage of ATP with liberation of equimolar amounts of ADP and inorganic phosphate, is strictly dependent for activity on divalent (Mg++ or Mn++) and monovalent (K+, Rb+, Csf, or NH4+) cations, and requires catalytic amounts of bicarbonate. A detailed consideration of these properties is presented for the enzyme purified approximately 150-fold from C. utilis. Urea amidolyase activity is induced in C. utilis by urea and other substances which most likely are enzymatically degraded to urea. Repression of the enzyme occurs when low evels of ammonia are present in the medium. Extracts of other yeasts, such as Candida flareri and Saccharomyces cerevisiae, as well as of the unicellular green algae Chlorella ellipsoidea, Chlorella pyrenoidosa, and Chlamydomonas reinhardtii, also contain urea amidolyase activity when these organisms are grown in media containing urea as the sole source of nitrogen.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Purification and properties of the urea amidolyase from Candida utilis.

Urea amidolyase was purified to homogeneity from extracts of Candida utilis. The purification involves protamine sulfate precipitation, ammonium sulfate precipitation, polyethylene glycol precipitation, Sepharose 6B gel filtration, DEAE-cellulose column chromatography, and hydroxylapatite column chromatography. The final preparation is pure as judged by disc-gel electrophoresis. The molecular w...

متن کامل

Urea amidolyase of Candida utilis. Characterization of the urea cleavage reactions.

Evidence is presented that the enzymes catalyzing the three reactions involved in urea cleavage in Candida utilis, biotin carboxylation, urea carboxylation, and allophanate hydrolysis occur as a complex of enzymes. The allophanate-hydrolyzing activity could not be separated from the urea-cleaving activity using common methods of protein purification. Further, urea cleavage and allophanate hydro...

متن کامل

Enhancement of L-asparaginase Production by Candida utilis in a 13L Fermenter and its Purification

L- asparaginase enzyme is a renown enzyme due to its chemotherapeutic properties. This enzyme could also be employed in food processing technology. The present study aimed, optimizing the agitation and aeration rate in L-asparaginase production, using Candida utilis, ATCC 9950 in batch fermentation system. Beet molasses used as the carbohydrate source for enzyme production. A maximum asparagina...

متن کامل

Acrylamide Reduction in Potato Crisps using: Asparaginase from Candida utilis, Commercial Asparaginase, Salt Immersion, and pH Treatment

This paper investigates the reduction of acrylamide formation in potato crisps as a result of asparaginase treatment, using calcium chloride and sodium chloride solutions with different concentrations, immersion in different pH solutions, and different frying conditions. The main aim is to compare the reduction of acrylamide in potato crisps using two kinds of asparaginase enzyme; the first enz...

متن کامل

Urea Amidolyase (DUR1,2) Contributes to Virulence and Kidney Pathogenesis of Candida albicans

The intracellular enzyme urea amidolyase (Dur1,2p) enables C. albicans to utilize urea as a sole nitrogen source. Because deletion of the DUR1,2 gene reduces survival of C. albicans co-cultured with a murine macrophage cell line, we investigated the role of Dur1,2p in pathogenesis using a mouse model of disseminated candidiasis. A dur1,2Δ/dur1,2Δ strain was significantly less virulent than the ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Journal of biological chemistry

دوره 247 13  شماره 

صفحات  -

تاریخ انتشار 1972