Biochemical Characterization of an Acid Phosphatase from<i>Thermus thermophilus</i>

Tham, Sy Jye; Chang, Chao-Pei Betty; Huang, Hao; Lee, Yueh Feng; Huang, Tze-Sing; Chang, Chung‐Liang

doi:10.1271/bbb.90773

Cited by 22 publications

(17 citation statements)

References 33 publications

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“…In addition, the enzyme was completely inhibited by sulfhydryl reagent 2-mercaptoethanol, a well-known thiol group inhibitor, which supports the possibility of involvement of sulfhydryl groups in the catalytic site of the enzyme [17,[24][25][26][27][28][29][30]. The metal-chelating agent EDTA did not inhibit the purified enzyme activity, suggesting the absence of any role of divalent cations for the activation of the enzyme.…”

Section: +mentioning

confidence: 65%

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Purification and Characterization of Acid Phosphatase from Monocrotophos (MCP) Hydrolyzing Aspergillus niger ITCC 7782.10 Isolated from Local Agricultural Field

Jain¹,

Garg²,

Dangwal³

et al. 2013

Turk J Bioch

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Section: +mentioning

confidence: 65%

“…Phosphatase activity of the enzyme preparation was determined by the modified method (without 0.12 mM Mg ++ ) of Tham [17]. The reaction mixture contained 100 µl of enzyme, 1 ml of 0.5 mM para nitro phenol phosphate (pNPP) and 1 ml 50 mM Tris-HCl buffer (pH-8).…”

Section: Phosphatase Assaymentioning

confidence: 99%

Purification and Characterization of Acid Phosphatase from Monocrotophos (MCP) Hydrolyzing Aspergillus niger ITCC 7782.10 Isolated from Local Agricultural Field

Jain¹,

Garg²,

Dangwal³

et al. 2013

Turk J Bioch

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“…However, other enzymes such as acid phosphatase or glucose-6-phosphate dehydrogenase have high turnover (ca 10 5 -10 6 sec ¡1 ), and conversion can be analyzed using common instrumentation. 19,20 Contrary to the use of enzymes in other diagnostic applications, enzymes expressed by phages only need to be viable within the duration of the assay. This requirement enables a large variety of high turnover enzymes to be considered in the design of the genetically engineered phage.…”

Section: Enzyme Optimizationmentioning

confidence: 99%

Engineering bacteriophage for a pragmatic low-resource setting bacterial diagnostic platform

2016

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Bacteriophages represent multifaceted building blocks that can be incorporated as substitutes for, or in unison with other detection methods, to create powerful new diagnostics for the detection of bacteria. The ease of phage manipulation, production, and detection speed clearly highlights that there remains unrealized opportunities to leverage these phage-based components in diagnostics amenable to resource-limited settings. The passage of regulations like the Food Safety Modernization act, and the ever increasing extent of global trade and travel, will create further demand for these types of diagnostics. While phage-based diagnostics have begun to entering the market place, further research is needed to ensure the potential benefits of phage-based technologies for public health are fully realized. We are just beginning to explore the possibilities that phage-based detection can offer us in the future. The combination of engineered phages as well as engineered enzymes could result in ultrasensitive detection systems for low-resource settings. Because the reporter enzyme is synthesized in vivo, we need to consider the options outside of normal enzyme reporters. In this case, common enzyme issues such as purification and long-term stability are less important. Phage-based diagnostics were conceptualized from out-of-the box thinking and the evolution of these systems should be as well.

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“…Cu 2þ , Zn 2þ , and Fe 3þ are common inhibitors for this enzyme. [3][4][5][6][7][8] In Vigna sinensis seeds, tomato cell cultures, tobacco cells and Arabidopsis, acid phosphatase activity was found to be enhanced or unaffected by Ca 2þ and Mg 2þ . [3,9] Furthermore, several reports in the literature have illustrated the interference of metal oxoanions (e.g., molybdate and vanadate) in catalytic activity of acid phosphatase.…”

Section: Introductionmentioning

confidence: 99%

The Inhibitory Effect of Metals and Other Ions on Acid Phosphatase Activity FromVigna aconitifoliaSeeds

Srivastava¹,

Anand²

2014

Preparative Biochemistry and Biotechnology

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Sensitivity of acid phosphatase from Vigna aconitifolia seeds to metal ions, fluoride, and phosphate was examined. All the effectors had different degree of inhibitory effect on the enzyme. Among metal ions, molybdate and ferric ion were observed to be most potent inhibitors and both exhibited mixed type of inhibition. Acid phosphatase activity was inhibited by Cu2+ in a noncompetitive manner. Zn and Mn showed mild inhibition on the enzyme activity. Inhibition kinetics analysis explored molybdate as a potent inhibitor for acid phosphatase in comparison with other effectors used in this study. Fluoride was the next most strong inhibitor for the enzyme activity, and caused a mixed type of inhibition. Phosphate inhibited the enzyme competitively, which demonstrates that inhibition due to phosphate is one of the regulatory factors for enzyme activity.

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Biochemical Characterization of an Acid Phosphatase fromThermus thermophilus

Cited by 22 publications

References 33 publications

Purification and Characterization of Acid Phosphatase from Monocrotophos (MCP) Hydrolyzing Aspergillus niger ITCC 7782.10 Isolated from Local Agricultural Field

Purification and Characterization of Acid Phosphatase from Monocrotophos (MCP) Hydrolyzing Aspergillus niger ITCC 7782.10 Isolated from Local Agricultural Field

Engineering bacteriophage for a pragmatic low-resource setting bacterial diagnostic platform

The Inhibitory Effect of Metals and Other Ions on Acid Phosphatase Activity FromVigna aconitifoliaSeeds

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