scholarly journals Effects of Escherichia coli Alkaline Phosphatase PhoA on the Mineralization of Dissolved Organic Phosphorus

Water ◽  
2021 ◽  
Vol 13 (23) ◽  
pp. 3315
Author(s):  
Yanwen Zhou ◽  
Tingxi Zhang ◽  
Shengyan Jin ◽  
Siyu Chen ◽  
Yinlong Zhang
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Alkaline Phosphatase ◽  
Reaction Time ◽  
Organic Phosphorus ◽  
Phosphorus Concentration ◽  
Inhibition Rate ◽  
Dissolved Organic Phosphorus ◽  
Independent Manner ◽  
Phosphate Monoesters

Alkaline phosphatases, which play the key role in the mineralization of organic phosphorus, have been grouped into three distinct families, PhoA, PhoX, and PhoD. PhoA is still an important component of the Pho regulon for many microbes although its distribution is not as wide as that of PhoX and PhoD. However, several questions remain unclear about the effect of PhoA mineralization of dissolved organic phosphorus. In this study, the role of Escherichia coli alkaline phosphatase PhoA (hereinafter referred to as PhoA) in the mineralization of different organic phosphorus including phosphate monoesters, phosphate diesters, and phytic acids was investigated. The influence of the reaction time, organic phosphorus concentration, and L-amino acid on PhoA mineralization was examined. The results show that PhoA specifically hydrolyzes phosphate monoesters except for phytic acid and the optimal reaction time is around 12 h. The PhoA mineralization rate of glucose 6-phosphate disodium (G6P), 5′-adenosine monophosphate (AMP), and sodium glycerophosphate (BGP) significantly decreased by 38.01%, 55.31%, and 57.08%, respectively (p < 0.01), while the concentration of organic phosphorus increased from 0.50 to 5.00 mg/L. Overall, L-amino acids inhibited PhoA mineralization in a concentration-independent manner. The inhibitory effect of neutral amino acids serine (L-Ser) and tyrosine (L-Tyr) was significantly higher than that of basic amino acids arginine (L-Arg), lysine (L-Lys), and histidine (L-His). All the five amino acids can inhibit PhoA mineralization of AMP, with the highest inhibition rate observed for L-Tyr (23.77%), the lowest—for L-Arg (1.54%). Compared with other L-amino acids, L-Tyr has the highest G6P and BGP mineralization inhibition rate, with the average inhibition rates of 12.89% and 11.65%, respectively. This study provides meaningful information to better understand PhoA mineralization.

scholarly journals Non-Conventional Metal Ion Cofactor Requirement of Dinoflagellate Alkaline Phosphatase and Translational Regulation by Phosphorus Limitation

2019 ◽  
Vol 7 (8) ◽  
pp. 232 ◽  
Author(s):  
Xin Lin ◽  
Chentao Guo ◽  
Ling Li ◽  
Tangcheng Li ◽  
Senjie Lin
Keyword(s):  
Alkaline Phosphatase ◽  
Metal Ion ◽  
Translational Regulation ◽  
Organic Phosphorus ◽  
Niche Differentiation ◽  
Phosphorus Limitation ◽  
Marine Phytoplankton ◽  
Phosphate Limitation ◽  
Dissolved Organic Phosphorus ◽  
Metal Cofactor

Alkaline phosphatase (AP) enables marine phytoplankton to utilize dissolved organic phosphorus (DOP) when dissolved inorganic phosphate (DIP) is depleted in the ocean. Dinoflagellate AP (Dino-AP) represents a newly classified atypical type of AP, PhoAaty. Despite While being a conventional AP, PhoAEC is known to recruit Zn2+ and Mg2+ in the active center, and the cofactors required by PhoAaty have been contended and remain unclear. In this study, we investigated the metal ion requirement of AP in five dinoflagellate species. After AP activity was eliminated by using EDTA to chelate metal ions, the enzymatic activity could be recovered by the supplementation of Ca2+, Mg2+ and Mn2+ in all cases but not by that of Zn2+. Furthermore, the same analysis conducted on the purified recombinant ACAAP (AP of Amphidinium carterae) verified that the enzyme could be activated by Ca2+, Mg2+, and Mn2+ but not Zn2+. We further developed an antiserum against ACAAP, and a western blot analysis using this antibody showed a remarkable up-regulation of ACAAP under a phosphate limitation, consistent with elevated AP activity. The unconventional metal cofactor requirement of Dino-AP may be an adaptation to trace metal limitations in the ocean, which warrants further research to understand the niche differentiation between dinoflagellates and other phytoplankton that use Zn–Mg AP in utilizing DOP.

scholarly journals Investigating effect of Amino Acids Leucine, Valine and Alanine on Alkaline Phosphatase Activity of purified Acetone fractions of Sweet Lemon, Garlic and Onion

2019 ◽  
Vol 10 (1) ◽  
pp. 34-38
Author(s):  
Ramin Tavakoli ◽  
Shahdokht Rastegar ◽  
Mansoor Khaledi ◽  
Ali Nouri ◽  
Mostafa Madmoli ◽  
...  
Keyword(s):  
Amino Acids ◽  
Alkaline Phosphatase ◽  
Allium Sativum ◽  
Organic Phosphorus ◽  
Enzyme Level ◽  
Citrus Limon ◽  
Inhibitory Effects ◽  
Saline Extract ◽  
Allium Cepa L ◽  
Alkaline Phosphate

Alkaline phosphatase enzyme (ALP, ALKP, ALPase, Alk Phos) (EC 3.1.3.1) produced by plants and microbes is presumed to convert organic phosphorus into available pi, which is absorbed by plants. Considering the importance of Alkaline phosphate enzyme and the balance between its function in the development of various diseases by increasing and decreasing the enzyme level by enzyme activating and regulating compounds, including amino acids and ions, which act as coenzyme and cofactor for the enzyme Can be a major role in Disease improvement. This study aims to comparatively investigate the inhibiting effect of the three Amino Acid as well as Alanine, Leucine and valine on Alkaline phosphatase was which extracted from Sweet Lemon (Citrus limon (L.) Osbeck), Garlic (Allium sativum L.) and Onion (Allium cepa L.). In this study, Leucine, Alanine and Valine amino acids showed strong inhibitory effects 23%, 26% and 34% respectively activity of Alkaline phosphatase obtained saline extract of plants Sweet Lemon, Garlic and Onion.  

Sign in / Sign up

Export Citation Format

Share Document