Cummins et al., 1999 - Google Patents
Zinc coordination and substrate catalysis within the neuropeptide processing enzyme endopeptidase EC 3.4. 24.15: identification of active site histidine and glutamate …Cummins et al., 1999
View HTML- Document ID
- 12487733782857720778
- Author
- Cummins P
- Pabon A
- Margulies E
- Glucksman M
- Publication year
- Publication venue
- Journal of Biological Chemistry
External Links
Snippet
Endopeptidase EC 3.4. 24.15 (EP24. 15) is a zinc metalloendopeptidase that is broadly distributed within the brain, pituitary, and gonads. Its substrate specificity includes a number of physiologically important neuropeptides such as neurotensin, bradykinin, and …
- HCHKCACWOHOZIP-UHFFFAOYSA-N zinc data:image/svg+xml;base64,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 data:image/svg+xml;base64,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 [Zn] 0 title abstract description 61
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
- C12N9/52—Proteinases Endopeptidases (3.4.21-3.4.25) derived from bacteria
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/90—Enzymes; Proenzymes
- G01N2333/914—Hydrolases (3)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES OR MICRO-ORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/34—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions involving hydrolase
- C12Q1/37—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions involving hydrolase involving peptidase or proteinase
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N27/00—Investigating or analysing materials by the use of electric, electro-chemical, or magnetic means
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Cummins et al. | Zinc coordination and substrate catalysis within the neuropeptide processing enzyme endopeptidase EC 3.4. 24.15: identification of active site histidine and glutamate residues | |
Franzke et al. | Antileukoprotease inhibits stratum corneum chymotryptic enzyme: evidence for a regulative function in desquamation | |
Keiler et al. | Identification of active site residues of the Tsp protease | |
Elrod-Erickson et al. | Binding Studies with Mutants of Zif268: Contribution of individual side chains to binding affinity and specificity in the Zif268 zinc finger-DNA complex | |
Rioli et al. | Novel natural peptide substrates for endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme | |
Bohacek et al. | Three-dimensional models of ACE and NEP inhibitors and their use in the design of potent dual ACE/NEP inhibitors | |
Juenemann et al. | Expanded polyglutamine-containing N-terminal huntingtin fragments are entirely degraded by mammalian proteasomes | |
Cuerrier et al. | Determination of peptide substrate specificity for μ-calpain by a peptide library-based approach: the importance of primed side interactions | |
Elce et al. | Autolysis, Ca2+ requirement, and heterodimer stability in m-calpain | |
Jirácek et al. | Development of Highly Potent and Selective Phosphinic Peptide Inhibitors of Zinc Endopeptidase 24-15 Using Combinatorial Chemistry (∗) | |
Colpas et al. | Identification of metal-binding residues in the Klebsiella aerogenes urease nickel metallochaperone, UreE | |
Fülöp et al. | Structures of prolyl oligopeptidase substrate/inhibitor complexes: use of inhibitor binding for titration of the catalytic histidine residue | |
Jiráček et al. | Development of the first potent and selective inhibitor of the zinc endopeptidase neurolysin using a systematic approach based on combinatorial chemistry of phosphinic peptides | |
Elmariah et al. | Cathepsin S signals via PAR2 and generates a novel tethered ligand receptor agonist | |
Sakata et al. | The squamous cell carcinoma antigen 2 inhibits the cysteine proteinase activity of a major mite allergen, Der p 1 | |
Arnold et al. | The interface between catalytic and hemopexin domains in matrix metalloproteinase-1 conceals a collagen binding exosite | |
Sun et al. | Importance of the P4′ residue in human granzyme B inhibitors and substrates revealed by scanning mutagenesis of the proteinase inhibitor 9 reactive center loop | |
Raymond et al. | Albumin is a substrate of human chymase: prediction by combinatorial peptide screening and development of a selective inhibitor based on the albumin cleavage site | |
Basak et al. | Inhibitory specificity and potency of proSAAS-derived peptides toward proprotein convertase 1 | |
Ascher et al. | Regulation of insulin-regulated membrane aminopeptidase activity by its C-terminal domain | |
Bianchi et al. | Complex formation between the hepatitis C virus serine protease and a synthetic NS4A cofactor peptide | |
Szabó et al. | High affinity small protein inhibitors of human chymotrypsin C (CTRC) selected by phage display reveal unusual preference for P4′ acidic residues | |
Kádas et al. | Narrow substrate specificity and sensitivity toward ligand-binding site mutations of human T-cell Leukemia virus type 1 protease | |
Krause et al. | MAPping the chiral inversion and structural transformation of a metal-tripeptide complex having Ni-superoxide dismutase activity | |
Santamaria et al. | Post-translational regulation and proteolytic activity of the metalloproteinase ADAMTS8 |