68 results about "Aspartate protease" patented technology

The invention relates to a method for the production of plants with increased protein content in leaves, by means of introduction of recombinant DNA molecules. Said recombinant DNA molecules are introduced into the plant, by means of a transformation system and comprise a DNA sequence of plant origin, expressed in plants, the genetic product of which inhibits a protein in leaves with the enzymatic activity of an aspartate protease and/or a serene protease. The plants which displays an increased content in leaf protein are chosen.

The present invention is directed to aspartic protease inhibitors represented by the following structural formula; or a pharmaceutically acceptable salt thereof. The present invention is also directed to pharmaceutical compositions comprising the aspartic protease inhibitors of Structural Formula (I). Methods of antagonizing one or more aspartic proteases in a subject in need thereof, and methods for treating an aspartic protease mediated disorder in a subject using these aspartic protease inhibitors are also disclosed.

Described are diaminopropanols of which are orally active and bind to renin to inhibit its activity. They are useful in the treatment or amelioration of diseases associated with elevated levels of renin activity or in the treatment of aspartic protease mediated disorders. Also described is a method for the use of the diaminopropanols in ameliorating or treating renin related disorders in a subject in need thereof.

The invention relates to compounds of formula (I):wherein R1 and R10 are each independently of the other lower alkoxycarbonyl; either R2, R3 and R4 are each independently of the other C1-C4alkyl and R7, R8 and R9 are each selected from hydrogen and C1-C4alkyl, with not more than 2 of the radicals being hydrogen; or R7, R8 and R9 are each independently of the other C1-C4alkyl and R2, R3 and R4 are each selected from hydrogen and C1-C4alkyl, with 1 or 2 of the radicals being hydrogen; R5 is phenyl or cyclohexyl; and R6 is phenyl or cyanophenyl; or salts thereof; those compounds are inhibitors of retroviral aspartate proteases and are effective, for example, against HIV.

The present invention discloses an antiviral feed additive for promoting the growth of soft-shelled turtles. The feed additive includes the following raw materials: Chinese scholartree leaf powder, aloe, rhizoma atractylodis, officinal magnolia bark, Indian fig, herba taching, herba portulacae, herba Houttuyniae, ginger powder, xylanase, aspartic proteases, mannanase, compound vitamin, compound amino acid, malic acid, maifanstone powder, sepiolite powder and bacillus subtilis. The feed additive has antiviral activity, and the feed can promote the growth of the soft-shelled turtles and reduce the morbidity of the soft-shelled turtles without residue, toxicity or side effects with the addition of the feed additive.

The present invention provides aminohydantoin anti-malarial agents. In some embodiments, these agents have the property of functions of targeting malarial aspartic proteases while at the same time having low activity against human BACE. Methods of employing such agents are also provided.

The invention relates to a preparation method of potato aspartic proteinase inhibitor and belongs to the technical field of bioactive products extracted from plant. The preparation method comprises the following steps: directly peeling, cutting and mixing potatoes evenly; carrying out high-speed centrifugation; completing high-pressure sterilization of the supernatant fluid and then carrying out high-speed centrifugation again; completing hyperfiltration and concentration; carrying out fractionated precipitation of ethanol; eliminating undissolved substance through centrifugation after deposition and redissolution; and finally, obtaining the dry powder of the aspartic proteinase inhibitor through vacuum freeze drying. The aspartic proteinase inhibitor prepared by the preparation method has higher inhibitory activity on pepsin and can be directly extracted from potatoes, thereby having low cost and application safety without causing pigment influence; therefore, the inhibitor has broad application prospects in the fields of foodstuff, medicament, agriculture, and the like.

The invention relates to a specific promoter of soybean seeds, which belongs to the sequence and use of a soybean aspartic protease gene promoter. The nucleotide sequence of the promoter is represented by the sequence No.1. The preparation method of the promoter comprises the following steps of: cloning the upstream distal sequence of gene soyAP1, analyzing the upstream sequence of the ATG of the gene soyAP1 and determining the deleted fragments SAP1, SAP2, soyAP1-p and SAP4; and amplifying the soyAP1-p fragment, linking the amplified fragment of the soyAP1-p with a cloning vector pMD 18-T, performing identification, measuring the sequence, and verifying the sequence. In the invention, the soyAP1-p promoter of soybean is cloned and expressed in the soybean seeds specifically, and the promoter obtained can be used as a favorable tool in researches on soybean transgenosis and particularly creates conditions for researching and developing soybean seed bioreactors.

The invention provides a bi-enzymatic hydrolysis method for preparing high-F-value oligopeptide crude liquid. The method includes steps: 1) pretreatment; 2) deodorization; 3) degreasing; 4) enzymolysis. The method has advantages that a pepsase enzyme activator and a flavourzyme enzyme activator are capable of activating pepsase and flavourzyme respectively to improve enzymolysis efficiency and shorten oligopeptide crude liquid preparation time; the pepsase which belongs to aspartic protease is inclined to shear an amino terminal or carboxyl terminal into aromatic amino acid, and aromatic amino acid residue exposure rate is high, so that exonuclease specific excision at the second step is facilitated; the flavourzyme is natural and safe and is exactly capable of serving as exonuclease to degrade bitter peptides obtained at first-step enzymolysis into amino acids. In addition, by terminal peptide hydrolysis, hydrolysis degree is raised.

The present invention relates to a method for modifying polyamide. The method comprises that polyamide is contacted with an enzyme preparation comprising an effective amount of protease enzyme in aqueous environment under conditions suitable for the function of the enzyme. The enzyme is preferably selected from the group of aspartic proteases, cysteine proteases and metallo-proteases.

The present invention provides an aspartic proteinase-inhibiting compound of the formula:

wherein a, b, c, d, and e, can be the same or different and each are R⁷, OR⁷, SR⁷, NR⁷R⁷, NHCOR⁷, CO₂R⁷, CN, NO₂, NH₂, N₃, or a halogen, wherein R⁷ and R⁸ are independently H or an alkyl. Substituents R¹ or R² are each H or an alkyl. Substituent R³ is a straight chain or branched alkyl, alkenyl, or alkynyl substituent, or is a cycloalkyl. Substituent A is OH, NH₂, or SH.

Further provided are pharmaceutical compositions, which include a therapeutically effective amount of at least one of the foregoing compounds, and therapeutic methods of using the foregoing compounds.

Disclosed is a method for evaluating enzyme inhibitory activity of a known or putative inhibitor or modulator of an enzyme. The enzymes under investigation are those having a low-barrier hydrogen bond present in an active site of the enzyme. The compound whose activity is to be evaluated is contacted to an enzyme having a low-barrier hydrogen bond present in an active site of the enzyme. The presence, absence, or electronic character of the low-barrier hydrogen bond is then measured. The method is useful for designing mechanistic-based inhibitors or modulators of aspartic proteases and other enzymes.

The invention discloses a production method and applications of a novel rhizomucor miehei aspartic protease, and particularly relates to a recombinant aspartic protease, a coding gene, and a production method and applications of the recombinant aspartic protease. The recombinant aspartic protease is protein having an amino acid sequence shown as SEQ ID NO:1. The coding gene of the recombinant aspartic protease is a DNA molecule shown as SEQ ID NO:2. An aspartic protease gene that is RmproA of rhizomucor miehei is connected to a pichia pastoris GS115 expression vector pPIC9K, and is converted into pichia pastoris and induced expression is performed to obtain the recombinant aspartic protease. Through high-density fermentation in a fermentation tank having a volume of 5 L, the maximum protease production activity at 156 h of a recombinant strain is 3400 U/mL, and the protein content is 6.42 mg/mL. The recombinant aspartic protease is capable of effectively tendering pork, reducing shearing force, making meat palatable, and effectively hydrolyzing animal and plant protein to prepare low-molecular-weight polypeptides.

A method of providing polypeptide preparations having a reduced content of undesired enzymatic side activities, the method comprising subjecting a medium containing a desired polypeptide such as an enzyme, a pharmaceutically active or immunologically active polypeptide to a pH of less than 2 for a period of time that is required to inactivate the side activities whilst retaining the activity of the desired polypeptide. The method is useful for providing milk clotting enzyme products including rennets or coagulants based on chymosin or pepsin or microbial aspartic proteases e.g. derived from bacterial species and species of filamentous fungi.

An aspect of the present invention is the use of a preparation containing a phytepsin, more specifically a cyprosin, containing the heterodimer, its N-terminal pro-peptide, the mature N-terminal peptide, and mature C-terminal peptide, as well as other precursor species, processing products, and aggregate species, either isolated or in any combinations of the former, native, extracted and partially purified from flowers of Cynara cardunculus, or recombinant, extracted from the supernatant from a culture of Saccharomyces cereviseae genetically modified for the heterologous production of cyprosin, for therapeutic applications more precisely for its use as an antitumor agent.

The present invention is directed to aspartic protease inhibitors. Certain aspartic protease inhibitors of the invention can be represented by the following structural formula or a pharmaceutically acceptable salt thereof. The present invention is also directed to pharmaceutical compositions comprising the disclosed aspartic protease inhibitors. The present invention is further directed to methods of antagonizing one or more aspartic proteases in a subject in need thereof, and methods for treating an aspartic protease mediated disorder in a subject using the disclosed aspartic protease inhibitors.

The invention relates to a substituted triaminotriazine compound and its preparation method and use in pharmacy. The substituted triaminotriazine compound has a general structural formula shown in the following description, and in the formula, R1 represents substituted phenyl ring and R2 represents substituted aromatic ring, naphthalene ring or heterocyclic aromatic. Through structure-based virtual screening and further structure reconstruction, the novel substituted triaminotriazine compound is synthesized. The novel substituted triaminotriazine compound is a fungus Sap2 inhibitor with a novel structure, has good enzyme inhibition activity and nematode in-vivo antifungal activity, provides a novel approach for deep research and development of novel-structure antifungal drugs and can be used for preparation of antifungal drugs and drugs for combination with the existing antibacterial drugs.

The invention provides aspartic protease and an encoding gene and an application thereof. The aspartic protease is a protein shown as (a) or (b), wherein (a) is constituted by an amino acid residue sequence shown as SEQ ID NO:3, or (b) is obtained by performing substitution and/or deletion and/or addition of one or more amino acid residues on the amino acid residue sequence shown as SEQ ID NO:3, has the functions of the aspartic protease and is derived from (a). Through a gene engineering technology, an aspartic protease gene is amplified from Geomycespannorum, and is transferred into Aspergillus oryzae, thereby realizing successful heterologous expression. The aspartic protease provided by the invention has a relatively high optimal reaction temperature, high thermal stability and a good industrial application prospect.

The present invention is directed to aspartic protease inhibitors. The present invention is also directed to pharmaceutical compositions comprising the disclosed aspartic protease inhibitors. The present invention is further directed to methods of antagonizing one or more aspartic proteases in a subject in need thereof, and methods for treating an aspartic protease mediated disorder in a subject using the disclosed aspartic protease inhibitors.