Skip Navigation

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
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 Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by MIYAJIMA, R.
Right arrow Articles by SHIIO, I.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by MIYAJIMA, R.
Right arrow Articles by SHIIO, I.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1968, Vol. 63, No. 2 139-148
© 1968 Japanese Biochemical Society

research-article

Regulation of Aspartate Family Amino Acid Biosynthesis in Brevibacterium flavum

I. Inhibition by Amino Acids of the Enzymes in Threonine Biosynthesis

RYUICHI MIYAJIMA, SHIN-ICHIRO OTSUKA and ISAMU SHIIO

From the Central Research Laboratories of Ajinomoto Co., Inc. Kawasaki

1. Effect of 13 amino acids on enzymes in the pathway from aspartate to threonine in Brevibacterium flavum were estimated.

2. Simultaneous addition of threonine and lysine (10 mM each) caused 56% inhibition of aspartate kinase [EC 2.7.2.4 [EC] ], whereas addition of either amino acid did not cause significant inhibitory effect.

3. L-Aspartate-ß-semialdehyde dehydrogenase [EC 1.2.1.11 [EC] ] was scarcely inhibited by amino acids of aspartate family. Serine inhibited the activity by about 40% at a concentration of 10 mM.

4. Homoserine dehydrogenase [EC 1.1.1.3 [EC] ] was competitively inhibited by threonine and by isoleucine. 3.3 mM of threonine inhibited the activity completely in the forward and reverse reaction, and 10 mM of isoleucine inhibited the activity by about 90% in the forward reaction, and by about 60% in the reverse reaction.

5. Homoserine kinase [EC 2.7.1.39 [EC] ] was inhibited by threonine in the extent of 60% at 30 mM. Other amino acids of aspartate family showed slightly inhibitory effect at 10 mM.

6. Threonine synthase [EC 4.2.99.2 [EC] ] was scarcely inhibited by amino acids of aspartate family. Cysteine and glutathione showed 100% inhibition at 10 mM revealed by measurement of the determination of phosphohomoserine disappearance.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 ScienceHome page
P. Datta
Regulation of Branched Biosynthetic Pathways in Bacteria
Science, August 8, 1969; 165(3893): 556 - 562.
[PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.