Literature DB >> 15303275

The 10 C-terminal residues of HTLV-I protease are not necessary for enzymatic activity.

Bryan E Herger1, Victoria L Mariani, KellyJ Dennison, Suzanne B Shuker.   

Abstract

Sequence alignment of human T-lymphotropic virus type I (HTLV-I) protease and other retroviral proteases reveals that the leukemia virus proteases contain residues at the C-terminus that are absent in the other proteases. We have prepared a mutant of HTLV-I protease that does not contain the 10 C-terminal residues and demonstrated that the catalytic efficiency of cleavage of a peptide substrate is unaffected.

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Year:  2004        PMID： 15303275     DOI： 10.1016/j.bbrc.2004.06.087

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


  3 in total

1.  Total chemical synthesis of human T-cell leukemia virus type 1 protease via native chemical ligation.

Authors:  Changqing Li; Xiangqun Li; Wuyuan Lu
Journal:  Biopolymers       Date:  2010       Impact factor: 2.505

2.  Crystal structure of human T cell leukemia virus protease, a novel target for anticancer drug design.

Authors:  Mi Li; Gary S Laco; Mariusz Jaskolski; Jan Rozycki; Jerry Alexandratos; Alexander Wlodawer; Alla Gustchina
Journal:  Proc Natl Acad Sci U S A       Date:  2005-12-13       Impact factor: 11.205

3.  C-terminal residues of mature human T-lymphotropic virus type 1 protease are critical for dimerization and catalytic activity.

Authors:  János Kádas; Péter Boross; Irene T Weber; Péter Bagossi; Krisztina Matúz; József Tözsér
Journal:  Biochem J       Date:  2008-12-15       Impact factor: 3.857
  3 in total

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