A Caltech Library Service

The d-amino acid oxidase of Neurospora

Horowitz, N. H. (1944) The d-amino acid oxidase of Neurospora. Journal of Biological Chemistry, 154 (1). pp. 141-149. ISSN 0021-9258.

PDF - Published Version
See Usage Policy.


Use this Persistent URL to link to this item:


Among artificially produced mutants of the mold Neurospora have been found strains lacking the ability to synthesize specific amino acids (1, 2). In the course of biochemical and genetic studies of this group of mutants it was observed that some of the mutants, e.g. those deficient in methionine, leucine, and arginine,(1) are able to utilize racemic mixtures of the amino acids with the same efficiency as the l, or physiologically occurring, forms. In the cases of the leucine- and the methionine-requiring mutants it was also possible to show utilization of the ar-keto analogues. It thus appeared possible that the mode of conversion of the d to the l isomers consists in oxidative deammation, followed by resynthesis. A study was therefore undertaken to test the ability of Neurospora to oxidize the “unnatural” optical isomers of the amino acids. It was found that extracts of the mold contain a d-amino acid oxidase similar in its action to the d-amino acid oxidase of mammalian kidney and liver (3). This finding supports the above hypothesis for the conversion of the d- to the l-amino acids. Since it appears that the d-amino acid oxidase has not been previously described in fungi, a number of experiments were performed on the Neurospora enzyme, the results of which are reported here.

Item Type:Article
Related URLs:
URLURL TypeDescription
Additional Information:© 1944 American Society of Biological Chemists. Received for publication, March 9, 1944. This work was supported by grants from the Rockefeller Foundation. The author is indebted to Dr. David Bonner for samples of the following amino acids: dl-proline, dl-N-methylleucine, dl-N,N-dimethylleucine, and dl-β,β-dimethyl-α-amino-n-butyric acid. A sample of d(-)-alanine was generously provided by Professor M.S. Dunn of the University of California, Los Angeles.
Funding AgencyGrant Number
Rockefeller FoundationUNSPECIFIED
Issue or Number:1
Record Number:CaltechAUTHORS:HORjbc44
Persistent URL:
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:11855
Deposited By: Tony Diaz
Deposited On:10 Oct 2008 04:03
Last Modified:03 Oct 2019 00:23

Repository Staff Only: item control page