Biosynthesis of leupeptin. II. Purification and properties of leupeptin acid synthetase.
- 1 January 1979
- journal article
- research article
- Published by Japan Antibiotics Research Association in The Journal of Antibiotics
- Vol. 32 (5) , 523-530
- https://doi.org/10.7164/antibiotics.32.523
Abstract
An enzyme which condenses acetyl-L-leucyl-L-leucine and L-arginine into acetyl-L-leucyl-L-leucyl-L-arginine (leupeptin acid) was partially purified from a cell extract of Streptomyces roseus MA839-A1. With respect to this catalytic activity, the enzyme showed the following characteristics: ATP is essential; optimum pH is 9.5; the activity is inhibited by EDTA or pyrophosphate or N-ethylmaleimide. The MW of the enzyme is about 260,000 daltons. It also catalyzes some other extension reactions, such as, acetyl-L-leucine + L-leucine + L-arginine .fwdarw. leupeptin acid, and acetyl-L-leucine + L-leucine .fwdarw. acetyl-L-leucyl-L-leucine, but neither L-leucine + L-arginine .fwdarw. (L-leucyl)1-2-L-arginine, nor acetyl-L-leucine + L-arginine .fwdarw. acetyl-L-leucyl-L-arginine. ATP-PPi exchange, catalyzed by this enzyme, proceeds with acetyl-L-leucine, or acetyl-L-leucyl-L-leucine or L-leucine, but not with acetate or arginine.This publication has 0 references indexed in Scilit: