Literature DB >> 3977895

Acylpeptide hydrolase activity from erythrocytes.

W M Jones, J M Manning.   

Abstract

Acylpeptide hydrolase, which cleaves the NH2-terminal acetylated or formylated amino acid from a blocked peptide, has been purified to apparent homogeneity from human erythrocytes. The enzyme catalyzes the hydrolysis of a diverse number of peptides and displays different pH optima for certain substrates in doing so. Zinc inhibits to the same extent the hydrolysis of both the most efficient and the least efficient substrates. This enzyme may play a pivotal role in the processing of polypeptide chains during biosynthesis.

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Year:  1985        PMID： 3977895     DOI： 10.1016/0006-291x(85)90275-x

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


  4 in total

Review 1.  The metabolic serine hydrolases and their functions in mammalian physiology and disease.

Authors:  Jonathan Z Long; Benjamin F Cravatt
Journal:  Chem Rev       Date:  2011-06-23       Impact factor: 60.622

2.  Genetic relationship between acylpeptide hydrolase and acylase, two hydrolytic enzymes with similar binding but different catalytic specificities.

Authors:  W M Jones; A Scaloni; F Bossa; A M Popowicz; O Schneewind; J M Manning
Journal:  Proc Natl Acad Sci U S A       Date:  1991-03-15       Impact factor: 11.205

3.  Specificity determinants of acylaminoacyl-peptide hydrolase.

Authors:  R G Krishna; F Wold
Journal:  Protein Sci       Date:  1992-05       Impact factor: 6.725

4.  Internalization of Erythrocyte Acylpeptide Hydrolase Is Required for Asexual Replication of Plasmodium falciparum.

Authors:  Rubayet Elahi; Christie Dapper; Michael Klemba
Journal:  mSphere       Date:  2019-05-08       Impact factor: 4.389
  4 in total

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