JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Negri, A.
Right arrow Articles by Williams, C. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Negri, A.
Right arrow Articles by Williams, C. H., Jr
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J. Biol. Chem., Vol. 262, Issue 21, 10026-10034, 07, 1987

D-aspartate oxidase from beef kidney. Purification and properties

A Negri, V Massey and CH Williams Jr

The flavoprotein D-aspartate oxidase (EC 1.4.3.1) has been purified to homogeneity from beef kidney cortex. The protein is a monomer with a molecular weight of 39,000 containing 1 molecule of flavin. The enzyme as isolated is a mixture of a major active form containing FAD and a minor inactive form containing 6-hydroxy-flavin adenine dinucleotide (6- OH-FAD). The absorption and fluorescence spectral properties of the two forms have been studied separately after reconstitution of the apoprotein with FAD or 6-OH-FAD, respectively. FAD-reconstituted D- aspartate oxidase has flavin fluorescence, shows characteristic spectral perturbation upon binding of the competitive inhibitor tartaric acid, is promptly reduced by D-aspartic acid under anaerobiosis, reacts with sulfite to form a reversible covalent adduct, stabilizes the red anionic form of the flavin semiquinone upon photoreduction, and yields the 3,4-dihydro-FAD-form after reduction with borohydride. A Kd of 5 X 10(-8) M was calculated for the binding of FAD to the apoprotein. 6-OH-FAD-reconstituted D-aspartate oxidase has no flavin fluorescence, shows no spectral perturbation in the presence of tartaric acid, is not reduced by D-aspartic acid under anaerobiosis, does not stabilize any semiquinone upon photoreduction, and does not yield the 3,4-dihydro-form of the coenzyme when reduced with borohydride; the enzyme stabilizes the p-quinoid anionic form of 6- OH-FAD and lowers its pKa more than two pH units below the value observed for the free flavin. The general properties of the enzyme thus resemble those of the dehydrogenase/oxidase class of flavoprotein, particularly those of the amino acid oxidases.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J BiochemHome page
A. Yamamoto, H. Tanaka, T. Ishida, and K. Horiike
Functional and Structural Characterization of D-Aspartate Oxidase from Porcine Kidney: Non-Michaelis Kinetics due to Substrate Activation
J. Biochem., March 1, 2007; 141(3): 363 - 376.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. R. Marshall, M. Gong, L. Wodke, J. H. Lamb, D. J. L. Jones, P. B. Farmer, N. S. Scrutton, and A. W. Munro
The Human Apoptosis-inducing Protein AMID Is an Oxidoreductase with a Modified Flavin Cofactor and DNA Binding Activity
J. Biol. Chem., September 2, 2005; 280(35): 30735 - 30740.
[Abstract] [Full Text] [PDF]

Home page
 J BiochemHome page
S. Takahashi, T. Takahashi, Y. Kera, R. Matsunaga, H. Shibuya, and R.-h. Yamada
Cloning and Expression in Escherichia coli of the D-Aspartate Oxidase Gene from the Yeast Cryptococcus humicola and Characterization of the Recombinant Enzyme
J. Biochem., April 1, 2004; 135(4): 533 - 540.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Sacchi, S. Lorenzi, G. Molla, M. S. Pilone, C. Rossetti, and L. Pollegioni
Engineering the Substrate Specificity of D-Amino-acid Oxidase
J. Biol. Chem., July 19, 2002; 277(30): 27510 - 27516.
[Abstract] [Full Text] [PDF]

Home page
 EndocrinologyHome page
G. D'Aniello, A. Tolino, A. D'Aniello, F. Errico, G. H. Fisher, and M. M. Di Fiore
The Role of D-Aspartic Acid and N-Methyl-D-Aspartic Acid in the Regulation of Prolactin Release
Endocrinology, October 1, 2000; 141(10): 3862 - 3870.
[Abstract] [Full Text] [PDF]

Home page
 FASEB J.Home page
A. D’ANIELLO, M. M. DI FIORE, G. H. FISHER, A. MILONE, A. SELENI, S. D’ANIELLO, A. F. PERNA, and D. INGROSSO
Occurrence of D-aspartic acid and N-methyl-D-aspartic acid in rat neuroendocrine tissues and their role in the modulation of luteinizing hormone and growth hormone release
FASEB J, April 1, 2000; 14(5): 699 - 714.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
B. E. Reuber, C. Karl, S. A. Reimann, S. J. Mihalik, and G. Dodt
Cloning and Functional Expression of a Mammalian Gene for a Peroxisomal Sarcosine Oxidase
J. Biol. Chem., March 7, 1997; 272(10): 6766 - 6776.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1987 by the American Society for Biochemistry and Molecular Biology.