The 10 C-terminal residues of HTLV-I protease are not necessary for enzymatic activity.
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.
Georgia Institute of Technology, School of Chemistry and Biochemistry, Atlanta 30332-0400, USA.
Bryan E
BE
Herger
Victoria L
VL
Mariani
KellyJ
K
Dennison
Suzanne B
SB
Shuker
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000596:Amino Acids / Q000737:chemistry*; D001665:Binding Sites; D003198:Computer Simulation; D010450:Endopeptidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D004789:Enzyme Activation; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D015368:Human T-lymphotropic virus 1 / Q000201:enzymology* / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
D000596:Amino Acids; D011994:Recombinant Proteins; D010450:Endopeptidases