Shailaja, M. S. ; Raghavendra Rao, M. R. (1971) Homoserine dehydrogenases of Serratia marcescens Sa-3 Biochemical and Biophysical Research Communications, 45 (4). pp. 1089-1095. ISSN 0006-291X
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Official URL: http://linkinghub.elsevier.com/retrieve/pii/000629...
Related URL: http://dx.doi.org/10.1016/0006-291X(71)90449-9
Abstract
(i) At least two methionine-repressible HsDHs are present in S.marcescens Sa-5 and these account for the most (90%) of the HsDH activity, (ii) the NAD+-activity is completely, and the NADP+-HsDH strongly (75-80%) repressed by L-methionine, L-cysteine and L-homoserine, but both seem to be sensitive only to cysteine among the amino acids tested, (iii) the residual NADP+-activity persisting after growth in presence of L-methionine is inhibited 80% by 10 mM L-threonine and possibly this activity is distinct from the major NADP+-enzyme, and (iv) these HsDH activities are distinct from aspartokinase.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to Elsevier Science. |
| ID Code: | 33412 |
| Deposited On: | 30 Mar 2011 13:15 |
| Last Modified: | 09 Oct 2011 05:03 |
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