In situ kinetic measurements of d-amino acid oxidase in rat liver with respect to its substrate specificity

1993 ◽  
Vol 25 (8) ◽  
pp. 578-582 ◽  
Author(s):  
Wilma M. Frederiks ◽  
Cornelis J. F. Van Noorden ◽  
Frans Marx ◽  
Peter T. Gallagher ◽  
Brian P. Swann
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Rat Liver ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Kinetic Measurements

In situ kinetic measurements ofd-amino acid oxidase in rat liver with respect to its substrate specificity

1993 ◽  
Vol 25 (8) ◽  
pp. 578-582
Author(s):  
Wilma M. Frederiks ◽  
Cornelis J. F. Van Noorden ◽  
Frans Marx ◽  
Peter T. Gallagher ◽  
Brian P. Swann
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Rat Liver ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Kinetic Measurements

Engineering the Substrate Specificity of Porcine Kidney d-Amino Acid Oxidase by Mutagenesis of the “Active-Site Lid”

2006 ◽  
Vol 139 (5) ◽  
pp. 873-879 ◽  
Author(s):  
Chiaki Setoyama ◽  
Yasuzo Nishina ◽  
Hisashi Mizutani ◽  
Ikuko Miyahara ◽  
Ken Hirotsu ◽  
...  
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Active Site ◽  
Acid Oxidase ◽  
Porcine Kidney ◽  
Amino Acid Oxidase

Alteration of substrate specificity of fructosyl-amino acid oxidase from Fusarium oxysporum

2007 ◽  
Vol 74 (4) ◽  
pp. 813-819 ◽  
Author(s):  
Maki Fujiwara ◽  
Jun-ichi Sumitani ◽  
Shinji Koga ◽  
Issei Yoshioka ◽  
Takuji Kouzuma ◽  
...  
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Fusarium Oxysporum ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Fructosyl Amino Acid Oxidase

A quantitative histochemical study of D-amino acid oxidase activity in rat liver in relationship with feeding conditions.

1991 ◽  
Vol 39 (1) ◽  
pp. 81-86 ◽  
Author(s):  
H R Patel ◽  
W M Frederiks ◽  
F Marx ◽  
A J Best ◽  
C J Van Noorden
Keyword(s):  
Amino Acid ◽  
Rat Liver ◽  
Oxidase Activity ◽  
Specific Inhibitor ◽  
Physiological Role ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Specific Test ◽  
Final Reaction Product ◽  
Final Reaction

The histochemical method for the demonstration of D-amino acid oxidase activity in rat liver, based on the use of cerium ions and the diaminobenzidine-cobalt-hydrogen peroxide procedure, was improved by the application of unfixed cryostat sections and a semipermeable membrane interposed between section and gelled incubation medium. The amount of final reaction product precipitated in a granular form was about four times higher with this technique in comparison with conventional procedures using fixed sections and aqueous incubation media. The specificity of the reaction was proven by the 70% reduction of the amount of final reaction product when incubating in the presence of substrate and D,L-beta-hydroxybutyrate, a specific inhibitor of D-amino acid oxidase activity. Cytophotometric analysis of liver sections revealed that the specific test minus control reaction was linear with incubation time and section thickness. The Km value of the enzyme of 10.3 +/- 2.7 mM, as determined in periportal areas, is about five times the value found with biochemical methods in liver cell homogenates. The enzyme activity in periportal areas is about five times the activity in pericentral areas. Fasting (24 and 48 hr) induced a significant decrease in D-amino acid activity in periportal and pericentral areas. The possible physiological role of the enzyme in liver is discussed.

scholarly journals Engineering the Substrate Specificity ofd-Amino-acid Oxidase

2002 ◽  
Vol 277 (30) ◽  
pp. 27510-27516 ◽  
Author(s):  
Silvia Sacchi ◽  
Simona Lorenzi ◽  
Gianluca Molla ◽  
Mirella S. Pilone ◽  
Carlo Rossetti ◽  
...  
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Acid Oxidase ◽  
Amino Acid Oxidase
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