PMID- 15303275 OWN - NLM STAT- MEDLINE DCOM- 20040910 LR - 20190612 IS - 0006-291X (Print) IS - 0006-291X (Linking) VI - 320 IP - 4 DP - 2004 Aug 6 TI - The 10 C-terminal residues of HTLV-I protease are not necessary for enzymatic activity. PG - 1306-8 AB - 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. FAU - Herger, Bryan E AU - Herger BE AD - Georgia Institute of Technology, School of Chemistry and Biochemistry, Atlanta 30332-0400, USA. FAU - Mariani, Victoria L AU - Mariani VL FAU - Dennison, KellyJ AU - Dennison K FAU - Shuker, Suzanne B AU - Shuker SB LA - eng PT - Journal Article PL - United States TA - Biochem Biophys Res Commun JT - Biochemical and biophysical research communications JID - 0372516 RN - 0 (Amino Acids) RN - 0 (Recombinant Proteins) RN - EC 3.4.- (Endopeptidases) SB - IM MH - Amino Acid Sequence MH - Amino Acid Substitution MH - Amino Acids/*chemistry MH - Binding Sites MH - Computer Simulation MH - Endopeptidases/*chemistry/genetics/*metabolism MH - Enzyme Activation MH - Escherichia coli/enzymology/genetics MH - Human T-lymphotropic virus 1/*enzymology/genetics MH - *Models, Molecular MH - Molecular Sequence Data MH - Protein Binding MH - Protein Conformation MH - Recombinant Proteins/chemistry/metabolism MH - Sequence Homology, Amino Acid MH - Structure-Activity Relationship EDAT- 2004/08/12 05:00 MHDA- 2004/09/11 05:00 CRDT- 2004/08/12 05:00 PHST- 2004/08/12 05:00 [pubmed] PHST- 2004/09/11 05:00 [medline] PHST- 2004/08/12 05:00 [entrez] AID - S0006-291X(04)01344-0 [pii] AID - 10.1016/j.bbrc.2004.06.087 [doi] PST - ppublish SO - Biochem Biophys Res Commun. 2004 Aug 6;320(4):1306-8. doi: 10.1016/j.bbrc.2004.06.087.