Schechter et al., 2005 - Google Patents
Inhibition of human kallikreins 5 and 7 by the serine protease inhibitor lympho-epithelial Kazal-type inhibitor (LEKTI)Schechter et al., 2005
View PDF- Document ID
- 5634507211219574525
- Author
- Schechter N
- Choi E
- Wang Z
- Hanakawa Y
- Stanley J
- Kang Y
- Clayman G
- Jayakumar A
- Publication year
External Links
Snippet
LEKTI is a 120-kDa protein that plays an important role in skin development, as mutations affecting LEKTI synthesis underlie Netherton syndrome, an inherited skin disorder producing severe scaling. Its primary sequence indicates that the protein consists of 15 domains, all …
- 230000002401 inhibitory effect 0 title abstract description 162
Classifications
-
- 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)
- C12N9/64—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6424—Serine endopeptidases (3.4.21)
- C12N9/6427—Chymotrypsins (3.4.21.1; 3.4.21.2); Trypsin (3.4.21.4)
-
- 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)
- C12N9/58—Proteinases Endopeptidases (3.4.21-3.4.25) derived from fungi
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/81—Protease inhibitors
- C07K14/8107—Endopeptidase (E.C. 3.4.21-99) inhibitors
- C07K14/811—Serine protease (E.C. 3.4.21) inhibitors
- C07K14/8114—Kunitz type inhibitors
- C07K14/8117—Bovine/basic pancreatic trypsin inhibitor (BPTI, aprotinin)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/81—Protease inhibitors
- C07K14/8107—Endopeptidase (E.C. 3.4.21-99) inhibitors
- C07K14/8146—Metalloprotease (E.C. 3.4.24) inhibitors, e.g. tissue inhibitor of metallo proteinase, TIMP
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
- C12Y304/21—Serine endopeptidases (3.4.21)
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Schechter et al. | Inhibition of human kallikreins 5 and 7 by the serine protease inhibitor lympho-epithelial Kazal-type inhibitor (LEKTI) | |
Bangert et al. | Different N-terminal forms of α2-plasmin inhibitor in human plasma | |
Le Bonniec et al. | Glu-192----Gln substitution in thrombin mimics the catalytic switch induced by thrombomodulin. | |
Caughey et al. | Angiotensin II generation by mast cell α-and β-chymases | |
Söllner et al. | Isolation and characterization of hirustasin, an antistasin‐type serine‐proteinase inhibitor from the medical leech Hirudo medicinalis | |
Andreasen et al. | Plasminogen activator inhibitor type‐1: reactive center and amino‐terminal heterogeneity determined by protein and cDNA sequencing | |
Travis et al. | Isolation and properties of recombinant DNA produced variants of human alpha 1-proteinase inhibitor. | |
Maubach et al. | The inhibition of cathepsin S by its propeptide—specificity and mechanism of action | |
Jean et al. | Enzymic characterization of murine and human prohormone convertase-1 (mPC1 and hPC1) expressed in mammalian GH4C1 cells | |
Desrochers et al. | Interstitial collagenase (matrix metalloproteinase-1) expresses serpinase activity. | |
Han et al. | The protein Z-dependent protease inhibitor is a serpin | |
Schechter et al. | Reaction of human chymase with reactive site variants of alpha 1-antichymotrypsin. Modulation of inhibitor versus substrate properties. | |
Yoshida et al. | Substrate specificity of two chymotrypsin-like proteases from rat mast cells. Studies with peptide 4-nitroanilides and comparison with cathepsin G | |
Caughey et al. | Dog mastocytoma tryptase: affinity purification, characterization, and amino-terminal sequence | |
Shieh et al. | The reactive site of human alpha 2-antiplasmin. | |
Schatteman et al. | Proteolytic activation of purified human procarboxypeptidase U | |
Cardozo et al. | A 3, 4-dichloroisocoumarin-resistant component of the multicatalytic proteinase complex | |
Patston et al. | Reactivity of alpha 1-antitrypsin mutants against proteolytic enzymes of the kallikrein-kinin, complement, and fibrinolytic systems. | |
Miyata et al. | Coagulation factor XII (Hageman factor) Washington DC: inactive factor XIIa results from Cys-571----Ser substitution. | |
Potempa et al. | An elastase inhibitor from equine leukocyte cytosol belongs to the serpin superfamily. Further characterization and amino acid sequence of the reactive center. | |
TRAVIS et al. | Kinetic studies on the interaction of α 1-proteinase inhibitor (Pittsburgh) with trypsin-like serine proteinases | |
Sun et al. | Production and characterization of recombinant human proteinase inhibitor 6 expressed in Pichia pastoris | |
Welch et al. | Purification of Human Matrilysin Produced inEscherichia coliand Characterization Using a New Optimized Fluorogenic Peptide Substrate | |
Walter et al. | Highly efficient inhibition of human chymase by α (2)-macroglobulin | |
FUKASAWA et al. | Aminopeptidase B is structurally related to leukotriene-A4 hydrolase but is not a bifunctional enzyme with epoxide hydrolase activity |