Improved purification, amino acid analysis and molecular weight of homogeneous d-amino acid oxidase from pig kidney

1973 ◽  
Vol 327 (2) ◽  
pp. 266-273 ◽  
Author(s):  
Bruno Curti ◽  
Severino Ronchi ◽  
Umberto Branzoli ◽  
Giuseppina Ferri ◽  
Charles H. Williams
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Analysis ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Pig Kidney

Molecular weight and configuration of d-amino acid oxidase protein

1961 ◽  
Vol 54 (1) ◽  
pp. 199-201 ◽  
Author(s):  
Kunio Yagi ◽  
Takayuki Ozawa ◽  
Tatsuo Ooi
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Acid Oxidase ◽  
Amino Acid Oxidase

scholarly journals Studies on the active centre of Rhodotorula gracilisd-amino acid oxidase and comparison with pig kidney enzyme

1992 ◽  
Vol 286 (2) ◽  
pp. 389-394 ◽  
Author(s):  
L Pollegioni ◽  
S Ghisla ◽  
M S Pilone
Keyword(s):  
Amino Acid ◽  
Solvent Accessibility ◽  
Alkylating Agents ◽  
Fine Tuning ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Active Centre ◽  
Pig Kidney ◽  
Mammalian Enzyme ◽  
Active Centres

D-Amino acid oxidase (EC 1.4.3.3) from Rhodotorula gracilis has been reconstituted with 8-chloro-, 8-mercapto-, 6-hydroxy-, 2-thio-, 5-deaza- and 1-deaza-FAD, and the properties of the resulting complexes have been studied and compared with those of the correspondingly modified pig kidney D-amino acid oxidases. Binding appears to be tight for most analogues, at least as tight as for native FAD (approximately 10(-8) M). 8-Mercapto- and 6-hydroxy-FAD bind in their para- and ortho-quinoid forms respectively to yeast D-amino acid oxidase, inferring the presence of a positive charge near the flavin N(1) position, as in the case of the mammalian enzyme. On the other hand, important differences in active-site microenvironment emerge: solvent accessibility to flavin position 8 is drastically restricted in yeast D-amino acid oxidase as indicated by the unreactivity of 8-chloro- and 8-mercapto-FAD enzyme with thiolates and alkylating agents. Significantly different microenvironments are also likely to occur around the flavin positions N(1)-C(2) = 0, N(3)-H and N(5). This is deduced from the differences in interaction of the two proteins with 1-deaza-FAD, 5-deaza-FAD and 2-thio-FAD and from the properties of the respective complexes. The same re-side flavin stereospecificity as shown by the mammalian enzyme was determined for the yeast enzyme using 8-hydroxy-5-deaza-FAD. Thus we can deduce the presence of a similar pattern of functional groups at the active centres of the two enzymes, while the fine tuning of specificity and regulation correlate with environmental differences at specific flavin loci.

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