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The 10 C-terminal residues of HTLV-I protease are not necessary for enzymatic activity.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2004 Aug 06; Vol. 320 (4), pp. 1306-8. - Publication Year :
- 2004
-
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.
- Subjects :
- Amino Acid Sequence
Amino Acid Substitution
Binding Sites
Computer Simulation
Endopeptidases genetics
Enzyme Activation
Escherichia coli enzymology
Escherichia coli genetics
Human T-lymphotropic virus 1 genetics
Molecular Sequence Data
Protein Binding
Protein Conformation
Recombinant Proteins chemistry
Recombinant Proteins metabolism
Sequence Homology, Amino Acid
Structure-Activity Relationship
Amino Acids chemistry
Endopeptidases chemistry
Endopeptidases metabolism
Human T-lymphotropic virus 1 enzymology
Models, Molecular
Subjects
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 320
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 15303275
- Full Text :
- https://doi.org/10.1016/j.bbrc.2004.06.087