Mechanism of the salt activation of laccase Lac15

2020 ◽  
Vol 521 (4) ◽  
pp. 997-1002 ◽  
Author(s):  
Zhi Li ◽  
Sha Jiang ◽  
Yanan Xie ◽  
Zemin Fang ◽  
Yazhong Xiao ◽  
...  
Keyword(s):  
2006 ◽  
Vol 103 (15) ◽  
pp. 5706-5710 ◽  
Author(s):  
R. K. Eppler ◽  
R. S. Komor ◽  
J. Huynh ◽  
J. S. Dordick ◽  
J. A. Reimer ◽  
...  

1984 ◽  
Vol 233 (1) ◽  
pp. 212-218 ◽  
Author(s):  
Genichiro Oshima ◽  
Katsuhiko Akashi ◽  
Michiyuki Yamada

1980 ◽  
Vol 189 (1) ◽  
pp. 45-49 ◽  
Author(s):  
A L Fluharty ◽  
R L Stevens ◽  
R T Miller ◽  
H Kihara

The cholate and taurodeoxycholate activations of cerebroside sulphate sulphohydrolase (cerebroside-3-sulphate 3-sulphohydrolase, EC 3.1.6.8) activity of arylsulphatase A (aryl-sulphate sulphohydrolase, EC 3.1.6.1) were compared. Taurodeoxycholate caused a sharp peak of response at a concentration of 1.25 mg/ml (type-I activation). Cholate also showed type-I activation but, in addition, it evoked a second, higher, response plateau at concentrations between 5 and 10 mg/ml (type-II activation). At the pH of the reaction, cholate is converted largely to the sparingly soluble free aicd, so at the high concentrations associated with type-II activation, copious precipitates were formed. It was found that the precipitated material was essential for the type-II activation. Type-I activation appears to involve bile salt interaction with substrate, while type-II activation appears to involve enzyme interaction with solid-phase cholic acid. the putative mutant arylsulphatase A in an unusual form of metachromatic leukodystrophy hydolysed cerebroside sulphate only in the presence of high levels of cholate. The type-II activation may thus be simulating a physiological desulphation reaction.


1983 ◽  
Vol 6 (6) ◽  
pp. 501-506
Author(s):  
H. R. Lerner ◽  
Leonora Reinhold ◽  
Rachel Guy ◽  
Yael Braun ◽  
Miriam Hasidim ◽  
...  

2004 ◽  
Vol 85 (4) ◽  
pp. 456-459 ◽  
Author(s):  
John A. Morgan ◽  
Douglas S. Clark

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