Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving hydrolase
Reexamination Certificate
2005-05-03
2005-05-03
Wax, Robert A. (Department: 1653)
Chemistry: molecular biology and microbiology
Measuring or testing process involving enzymes or...
Involving hydrolase
C435S220000, C536S023700
Reexamination Certificate
active
06887677
ABSTRACT:
Compounds and methods for designing and identifying compounds which inhibit TFPP-like aspartyl protease enzymes by targeting the aspartic acid residues of the active site or mimicking peptides corresponding to the region surrounding the substrate's cleavage site are provided. Agents identified as inhibitors of TFPP-like aspartyl proteases such as type 4 prepilin peptidases are expected to be useful as anti-bacterial agents and in inhibiting development of drug resistant strains of bacteria.
REFERENCES:
patent: 5872210 (1999-02-01), Medabalimi
patent: 20020016296 (2002-02-01), Haass et al.
patent: 199 02 550 (2000-07-01), None
patent: WO 9512408 (1995-11-01), None
patent: WO 0043505 (2000-07-01), None
Billich et al., “Synthetic Peptides as Substrates and Inhibitors of Human Immune Deficiency Virus-1 Protease”, J. Biol. Chem. 1988 263(34):17905-17908 XP-002224206.
Humblet et al., “Characterization of two structurally novel HIV-1 protease inhibitors identified by rational selection”, Antiviral Research 1993 21:73-84 XP009002114.
Kaufman et al., “Processing of TCP pilin by TcpJ typifies a common step intrinsic to a newly recognized pathway of extracellular protein secretion by gram-negative bacteria”, Genes & Development 1991 5:1834-1846 XP009002002.
Kick et al., “Structure-based design and combinatorial chemistry yield low nanomolar inhibitors of cathepsin D”, Chemistry & Biology 1997 4(4):297-307 XP-002065985.
Sohail et al., “Thermostabilization of carboxymethylcellulase fromAspergillus nigerby carboxyl group modification”, Biotechnology Letters 1997 19(4):325-329 Database accession No. PREV19979952378 XP-002224404.
Strom et al., “Posttanslational processing of type IV prepilin and homologs by PilD ofPseudomonas aeruginosa”, Methods in Enzymology 1994 235:527-540 Database accession No. NLM8057924 XP002224403.
Toogood et al., “A pepstatin-insensitive aspartic proteinase from a thermophilicBacillussp.”, Biochem. J. 1995 307:783-789 xP009002116.
Alm et al., “Genes involved in the biogenesis and function of type-4 fimbriae inPseudomonas aeruginosa”, Gene1997 192:89-98.
Darzins et al., “Molecular genetic analysis of type-4 pilus biogenesis and twitching motility usingPseudomonas aeruginosaas a model system—a review1”, Gene1997 192:109-115.
Filloux et al., “GSP-dependent protein secretion in Gram-negative bacteria:the Xcp system ofPseudomonas aeruginosa”, FEMS Microbiology Reviews1998 22:177-198.
LaPointe et al., “The Type 4 Prepilin Peptidases Comprise a Novel Family of Aspartic Acid Proteases”,J. Biol. Chem.2000 275 (2):1502-1510.
Russell et al., “The PilE gene product ofPseudomonas aeruginosa, required for pilus biogenesis, shares amino acid sequence identity with the N-terminal of type 4 prepilin proteins”,Molecular Microbiology1994 13(6):973-985.
Database Swiss-Prot38. Accession No. P27717 and Q56668. “Type 4 prepilin-like proteins leader peptide processing enzyme”, Kaufman et al. 1992.
LaPointe Christian F.
Taylor Ronald K.
Licata & Tyrrell P.C.
Trustees of Dartmouth College
Wax Robert A.
LandOfFree
Compounds and methods for identifying compounds which... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Compounds and methods for identifying compounds which..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Compounds and methods for identifying compounds which... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3407813