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A peptidase in human platelets that deamidates tachykinins. Probable identity with the lysosomal "protective protein".

Jackman, H L, Tan, F L, Tamei, H, Beurling-Harbury, C, Li, X Y, Skidgel, R A, Erdös, E G·1990·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(19)38586-2
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Abstract

We discovered an enzyme in human platelets that deamidates substance P and other tachykinins. Because an amidated carboxyl terminus is important for biological activity, we purified and characterized this deamidase. The enzyme, released from human platelets by thrombin, was purified to homogeneity by ammonium sulfate precipitation, followed by chromatography on an octyl-Sepharose column and chromatofocusing on PBE 94. The purified enzyme exhibits esterase, peptidase, and deamidase activities. The peptidase activity (with furylacryloyl-Phe-Phe) is optimal at pH 5.0 while the esterase (benzoyl-tyrosine ethyl ester) and deamidase (D-Ala2-Leu5-enkephalinamide) activities are optimal at pH 7.0. With biologically important peptides, the enzyme acts both as a deamidase (substance P, neurokinin A, and eledoisin) and a carboxy-peptidase (with bradykinin, angiotensin I, substance P-free acid, oxytocin-free acid) at neutrality, although the carboxypeptidase action is faster at pH 5.5. Enkephalins, released upon deamidation of enkephalinamides, were not cleaved. Gly9-NH2 of oxytocin was released without deamidation. Peptides with a penultimate Arg residue were not hydrolyzed. Some properties of the deamidase are similar to those reported for cathepsin A. The deamidase is inhibited by diisopropylfluorophosphate, inhibitors of chymotrypsin-type enzymes, and mercury compounds while other inhibitors of catheptic enzymes, trypsin-like enzymes, and metalloproteases were ineffective. In gel fil…

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Metadata

Authors
Jackman, H. L., Tan, F. L., Tamei, H., Beurling-Harbury, C., Li, X. Y., Skidgel, R. A., & Erdös, E. G.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1990-07
Volume
265
Issue
19
Pages
11265-11272
ISSN
0021-9258
DOI
10.1016/s0021-9258(19)38586-2
Cited by
135
References
0
Language
en
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