Properties of adenosine deaminase fromCandida albicans

Challa, A; Johnson, Salynn; Robertson, Kesha; Gunasekaran, M.

doi:10.1002/(sici)1521-4028(199905)39:2<97::aid-jobm97>3.0.co;2-n

Cited by 4 publications

(7 citation statements)

References 6 publications

(6 reference statements)

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“…Among bacteria, the most active are Clostridium species (Clostridium histolyticum and Clostridium sporogenes). A lesser degree of activity is found in Pseudomonas and Bacillus (Kamala-Kannan et al, 2010;Kunert, 1982;Gottlieb and Ciferri, 1956;Bentley, 1953;Takikawa et al, 1979;Challa et al, 1999).…”

Section: Proteinmentioning

confidence: 99%

“…Table 1. Microorganisms capable of producing deamination enzymes (Kamala-Kannan et al, 2010;Kunert, 1982;Gottlieb and Ciferri, 1956;Bentley, 1953;Ohshima et al, 1978;Ohshima et al, 1991 andChalla et al, 1999 Ammonium disappearance and NO 3 accumulation were reported to be more rapid at 25 C than at 10 C (Warneke et al, 2011). Higher rates of nitrification are expected to occur in shallower water relative to the rates of nitrification occurring in deeper water where lower water temperatures exist.…”

Section: Ajabsmentioning

confidence: 99%

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Nitrification of Urea and Assimilation of Nitrate in Saturated Soils Under Aerobic Conditions

Ghaly

Ramakrishnan

2013

American Journal of Agricultural and Biological Sciences

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The aim of this study was to investigate nitrification activity of urea and the assimilation of nitrate in a well aerated soil using perfusion technique with addition of glucose as an energy and carbon source. In this study, urea was rapidly nitrified by the bacteria in the saturated soil but its course of transformation to NO 3 was not linear. There was an initial increase in the concentration of nitrite during the nitrification experiment which indicated that the conversion of nitrite to nitrate was appreciably slower than the rate of conversion of urea to nitrite. The rate of conversion of NH 4 + to NO 2 was faster than the rate of conversion of NO 2 to NO 3 in the first 12 days and as a result the nitrate concentration reached 2.72 µg/ml on the 12 th day. After day 12, the concentration of NH 4 + in solution declined significantly and the rate of conversion of NO 2 to NO 3 became faster than the rate of conversion of NH 4 + to NO 2 -. The concentration of NO 2 -N in the solution reached zero on the 23 rd day. The nitrification curve has the character of a sigmoid curve whose midpoint, which representing the most rapid rate of nitrification, fell at the point of half conversion of urea to nitrite. The curve asymptotically approaches a nitrate value that represents 98% conversion of urea into nitrate. The rest of the urea (NH 4 ) has presumably been synthesized into bacterial cells. The initial pH of the soil was 7.7 due to the presence of NH 4 which decreased gradually due to the production of NO 3 reaching 6.9 by day 23. A nitrate reduction was observed under aerobic conditions. Denitrification did not proceed according to the known fact that O 2 prevents the denitrifying organisms from producing the enzyme responsible for the process. The alternative pathway for nitrate reduction could be by assimilatory reduction where nitrate was converted to ammonium and then to cells. The removal of nitrate and production of ammonium caused a rise in the pH. The initial pH of the solution was 6.9 which increased with time reaching 7.3 by the 7 th day. The expected nitrate reduction was 50% according to the assumption, but the 59% nitrate reduction observed in the experiment suggests that more than 25% of glucose C was metabolized and less than 75% was oxidized, otherwise.

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Section: Proteinmentioning

confidence: 99%

Section: Ajabsmentioning

confidence: 99%

Nitrification of Urea and Assimilation of Nitrate in Saturated Soils Under Aerobic Conditions

Ghaly

Ramakrishnan

2013

American Journal of Agricultural and Biological Sciences

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“…For Bacillus cereus enzyme, the activity is stabilized by NH 4 + or K + , while it is irreversibly lost in the absence of these or a few other monovalent cations 37 . Activating compounds were also described for the enzymes from Argopecten irradians concentricus (NH 4 Cl, (NH 4 ) 2 SO 4 ) 38 , Candida albicans enzyme (8-aza-adenine, adenine, AMP, ATP, IMP, inosine, N-acetyl-D-glucosamine) 39 and Mus musculus (dibutyryl-cAMP) 40 . The value of pH optimum signifi cantly varies among enzymes from diff erent sources, but usually confi nes to the range between pH 5 and 8.…”

Section: Substrates Activating Compounds and Inhibitors Of Adenosinementioning

confidence: 99%

“…The value of pH optimum signifi cantly varies among enzymes from diff erent sources, but usually confi nes to the range between pH 5 and 8. The pH range to observe enzymatic activity was shown to be pH 5-9 for Bos taurus ADA 41 , pH 4-8 for Candida albicans 39 and pH 3.5-5.5 for Streptomyces sp. 32 enzyme.…”

Section: Substrates Activating Compounds and Inhibitors Of Adenosinementioning

confidence: 99%

“…As mentioned previously, MgCl 2 and CoSO 4 have a remarkable activating eff ect, whereas MnCl 2 shows a slight inhibitory eff ect on enzyme activity 36 . Candida albicans ADA is inhibited by 1-methyl adenosine, AMP, p-chloromercuribenzoate, p-hydroxymercuribenzoic acid and theophylline 39 . ADA from Argopecten irradians concentricus has been found sensitive to these inhibitors: 2'-deoxyinosine, 2-amino-4-hydroxypteridine, folic acid, hypoxanthine, inosine, p-chloromercuribenzoate and purine riboside 38 .…”

Section: Substrates Activating Compounds and Inhibitors Of Adenosinementioning

confidence: 99%

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Aminohydrolases Acting on Adenine, Adenosine and Their Derivatives

Pospíšilová¹,

Frébort²

2007

BIOMED PAP

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Background: Adenine and adenosine-acting aminohydrolases are important groups of enzymes responsible for the metabolic salvage of purine compounds. Several subclasses of these enzymes have been described and given current knowledge of the full genome sequences of many organisms, it is possible to identify genes encoding these enzymes and group them according to their primary structure. Methods and Results:This article is a short overview of the enzymes classifi ed as adenine and adenosine deaminase. It summarises knowledge of their occurrence, genetic basis and their catalytic and structural properties.Conclusions: These enzymes are constitutive components of purine metabolism and their impairment may cause serious medical disorders. In humans, adenosine deaminase defi ciency is linked to severe combined immunodefi ciency and as such the enzyme has been approved for the fi rst gene therapy trial. The role of these enzymes in plants is unclear, since the activity was has not been detected in extracts and putative genes have not been yet cloned and analyzed. A literature search and amino acid identity comparison show that Ascomycetes contain only adenine deaminase, but not adenosine deaminase, despite the fact that corresponding genes are annotated in databases as the adenosine cleaving enzymes because they share the same conserved domain.

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AMP deaminase and adenosine deaminase activities in liver and brain regions in acute ammonia intoxication and subacute toxic hepatitis

Kaminsky

Kosenko

2010

Brain Research

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Properties of adenosine deaminase fromCandida albicans

Cited by 4 publications

References 6 publications

Nitrification of Urea and Assimilation of Nitrate in Saturated Soils Under Aerobic Conditions

Nitrification of Urea and Assimilation of Nitrate in Saturated Soils Under Aerobic Conditions

Aminohydrolases Acting on Adenine, Adenosine and Their Derivatives

AMP deaminase and adenosine deaminase activities in liver and brain regions in acute ammonia intoxication and subacute toxic hepatitis

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