|
type |
Journal Article |
authors |
Schmidt, A. |
title |
A cysteine desulfhydrase from spinach leaves specific for D-cysteine |
journal |
Zeitschrift fuer Pflanzenphysiologie |
Activity |
4.4.1.15 |
ui |
qwertg |
year |
(1982) |
volume |
107 |
number |
3 |
pages |
301-12. |
| |
abstract |
Spinach leaves contain a cysteine desulfhydrase which degrades D-cysteine, but not L-cysteine to inorg. sulfide, NH3, and pyruvate. This enzyme behaves similarly to cysteine synthase in gel filtration methods which sep. mols. by mol. wt. However, it can be sepd. from cysteine synthase by using DEAE-cellulose column chromatog. A pH optimum of .apprx.8.5-9 and an apparent Km of 0.14 mM for D-cysteine were detd. Citric acid and EDTA did not inhibit this activity, and the enzyme was active without addn. of monovalent or divalent metals. These observations suggest a novel regulatory system in amino acid biosynthesis and(or) regulation by the corresponding D-stereoisomer.
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last changed |
2004/02/13 18:33 |
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