Deamidation of calmodulin at neutral and alkaline pH: Quantitative relationships between ammonia loss and the susceptibility of calmodulin to modification by protein carboxyl methyltransferase-Reference-Cited by-同舟云学术

Deamidation of calmodulin at neutral and alkaline pH: Quantitative relationships between ammonia loss and the susceptibility of calmodulin to modification by protein carboxyl methyltransferase

Published:1989-01 Issue:1 Volume:268 Page:276-286
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Johnson Brett A.,Shirokawa Jill M.,Aswad Dana W.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference38 articles.

1. The unusual substrate specificity of eukaryotic protein carboxyl methyltransferases

2. Formation of ∈-(aminosuccinyl)-lysine from ∈-aspartyl-lysine from bacitracin A, and from the cell walls of lactobacilli

3. Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation.

4. Protein carboxyl methyltransferase facilitates conversion of atypical L-isoaspartyl peptides to normal L-aspartyl peptides.

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