HORMONALLY INDUCED MODIFICATION OF HELA ALKALINE PHOSPHATASE WITH INCREASED CATALYTIC ACTIVITY

Isozymes ◽  
1975 ◽  
pp. 343-365 ◽  
Author(s):  
RODY P. COX ◽  
NIMAI K. GHOSH ◽  
KIRSTAN BAZZELL ◽  
MARTIN J. GRIFFIN
1995 ◽  
Vol 8 (9) ◽  
pp. 865-871 ◽  
Author(s):  
Chris G. Dealwis ◽  
Liqing Chen ◽  
Catherine Brennan ◽  
Wlodek Mandecki ◽  
Cele Abad-Zapatero

2000 ◽  
Vol 294 (1-2) ◽  
pp. 57-66
Author(s):  
S.J Iqbal ◽  
P Whitaker ◽  
S Holland ◽  
W Madira ◽  
T Davies

2021 ◽  
Author(s):  
Morito Sakuma ◽  
Shingo Honda ◽  
Hiroshi Ueno ◽  
Kentaro Miyazaki ◽  
Nobuhiko Tokuriki ◽  
...  

Enzymes inherently exhibit molecule-to-molecule heterogeneity in catalytic activity or function, which underlies the acquisition of new functions in evolutionary processes. However, correlations between the functional heterogeneity of an enzyme and its multi-functionality or promiscuity remain elusive. In addition, the modulation of functional heterogeneity upon genetic perturbation is currently unexplored. Here, we quantitatively analyzed functional heterogeneity in the wild-type and 69 single-point mutants of Escherichia coli alkaline phosphatase (AP) by employing single-molecule assay with a femtoliter reactor array device. Most mutant enzymes exhibited higher functional heterogeneity than the wild-type enzyme, irrespective of catalytic activity. These results indicated that the wild-type AP minimizes functional heterogeneity, and single-point mutations can significantly expand the span of functional heterogeneity in AP. Moreover, we identified a clear correlation between functional heterogeneity and promiscuous activities. These findings suggest that enzymes can acquire greater functional heterogeneity following marginal genetic perturbations that concomitantly promote catalytic promiscuity.


2021 ◽  
Author(s):  
Kayla Gentile ◽  
Ashlesha Bhide ◽  
Joshua Kauffman ◽  
Subhadip Ghosh ◽  
Subhabrata Maiti ◽  
...  

It is usually assumed that enzymes retain their native structure during catalysis. However, the aggregation and fragmentation of proteins can be difficult to detect and sometimes conclusions are drawn based on the assumption that the protein is in its native form. We have examined three model enzymes, alkaline phosphatase (AkP), hexokinase (HK) and glucose oxidase (GOx). We find that these enzymes aggregate or fragment after addition of chemical species directly related to their catalysis. We used several independent techniques to study this behavior. Specifically, we found that glucose oxidase and hexokinase fragment in the presence of D-Glucose but not L-glucose, while hexokinase aggregates in the presence of Mg2+ ion and either ATP or ADP at low pH. Alkaline phosphatase aggregates in the presence of Zn2+ ion and inorganic phosphate. The aggregation of hexokinase and alkaline phosphatase does not appear to attenuate their catalytic activity. Our study indicates that specific multimeric structures of native enzymes may not be retained during catalysis and suggests pathways for different enzymes to associate or separate over the course of substrate turnover.


Author(s):  
Alina Dora SAMUEL ◽  
Cornel DOMUŢA ◽  
Maria ŞANDOR ◽  
Adrian VUŞCAN

We have determined five enzymatic activities (actual and potential dehydrogenase, catalase, acid and alkaline phosphatase) and one nonenzymatic catalytic activity (H2O2 splitting in autoclaved samples) in the 0–10–, 10–20– and 20–30–cm layers of a brown luvic soil submitted to a complex irrigation and crop rotation (2– and 3–crop rotations) experiment. Each activity in both non-irrigated and irrigated soil under wheat and maize crops was significantly higher in the intermediate layer than in the upper, respectively deeper layers. Non-irrigation – in comparison with irrigation – resulted in significantly higher soil phosphatase activities in the 0–10–, 10–20– and 20–30–cm layers, whereas dehydrogenase and catalase activities were significantly higher in irrigated soil. The soil under wheat or maize was more enzyme-active in the 3– than in the 2–crop rotation and in the monoculture. In the monoculture and in the 2–crop rotation, higher enzymatic activities were registered under wheat than under maize. In the 3–crop rotation, higher enzymatic activities were recorded maize under wheat. The enzymatic indicators of soil quality decreased depending on the nature of crops and kind of irrigation in the following order: maize ( 3–crop rotation ) > wheat ( 3–crop rotation) > wheat ( 2–crop rotation ) > maize ( 2–crop rotation ) > wheat ( monoculture ) > maize ( monoculture ).


2002 ◽  
Vol 20 (6) ◽  
pp. 381-389 ◽  
Author(s):  
Xian-En Zhang ◽  
Yu-Hua Zhou ◽  
Zhi-Ping Zhang ◽  
Hui-Fang Xu ◽  
Wen-Hai Shao ◽  
...  

1991 ◽  
Vol 274 (1) ◽  
pp. 91-95 ◽  
Author(s):  
C Hummer ◽  
J L Millán

The catalytic activity of human placental alkaline phosphatase (PLAP) and germ cell alkaline phosphatase (GCAP) can be inhibited, through an uncompetitive mechanism, by L-Phe. GCAP is also selectively inhibited by L-Leu. Site-directed mutagenesis of five of the 12 residues which are different in PLAP and GCAP revealed that Gly429 is the primary determinant of GCAP inhibition by L-Leu, and Ser84 and Leu297 play a modulatory role in the inhibition.


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