Elucidation of the cause for reduced activity of abnormal human plasmin containing an Ala55-Thr mutation: importance of highly conserved Ala55in serine proteases-Reference-Cited by-同舟云学术

Elucidation of the cause for reduced activity of abnormal human plasmin containing an Ala55-Thr mutation: importance of highly conserved Ala55in serine proteases

Published:1998-04-03 Issue:3 Volume:425 Page:448-452
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Takeda-Shitaka Mayuko,Umeyama Hideaki

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(98)00280-4/fullpdf

Reference31 articles.

1. The Three-Dimensional Structure of Asn 102 Mutant of Trypsin: Role of Asp 102 in Serine Protease Catalysis

2. The Catalytic Role of the Active Site Aspartic Acid in Serine Proteases

3. An investigation into the minimum requirements for peptide hydrolysis by mutation of the catalytic triad of trypsin

4. An alternate geometry for the catalytic triad of serine proteases

5. Charge state of His-57-Asp-102 couple in a transition state analogue-trypsin complex: a molecular orbital study.

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