74 results about "Enzyme specificity" patented technology

Enzyme substrates and associated technology of the present invention are provided. An enzyme substrate of the invention may comprise a biologically functional fluorescent dye and an enzyme-specific substrate moiety attached in such a way that the functionality of the functional dye is diminished. An enzymatic reaction may cleave at least a portion of the substrate moiety from the enzyme substrate to provide a more functional product dye. This product dye may be nonfluorescent or weakly fluorescent, in general, and relatively fluorescent, in a particular condition, such as when bound to a partner biological molecule or an assembly of partner biological molecules. An enzyme substrate of the present invention may thus be useful in fluorescence detection, and / or in any of a variety of useful applications, such as the detection of enzymatic activity in a cell-free system or in a living cell, the screening of drugs, or the diagnosis of disease.

The present invention relates to prodrug molecules comprising conjugates of an antiproliferative drug, a protease specific cleavable peptide, and, optionally, a targeting peptide, with the prodrugs being substantially inactive prior to degradation of the cleavable sequence by proteolytic enzymes abundant within or in close proximity to the target cancer cell. Also, pharmaceutical compositions of the conjugates and the use of these compositions for treatment of cancer are disclosed.

There is provided a method for specifically determining a glycated β-chain N-terminal of glycated hemoglobin using enzymes without a separation operation, and a determination reagent kit therefor. A protease that cleaves a glycated amino acid and / or a glycated peptide from a glycated β-chain N-terminal without substantially cleaving a glycated amino acid or a glycated peptide from a glycated α-chain N-terminal of glycated hemoglobin or a fragment thereof is screened. The method of specifically determining a glycated β-chain N-terminal of glycated hemoglobin and the determination reagent kit are provided by using the protease obtained by the screening method. According to the present invention, a glycated β-chain N-terminal of glycated hemoglobin can specifically be determined without a separation operation.

The invention relates to a substrate and an internal standard used in mass spectrography detection. The inventive substrate is provided which includes a substrate compound of formula A - B<1> - B<2> - B<3>: wherein A is a sugar moiety; B<1> is a linker moiety allowing the conjugation of moiety A and the remaining structure of the substrate; B<2> contains a permanently charged element such as a quaternary ammonium group so as to increase proton affinities and ionization efficiencies for mass spectrometry analysis; and B<3> of various carbon length conferring specificities to targeted enzymes. Also provided is a process to detect lysosomal diseases by contacting a sample with the inventive substrate along with an internal standard which is isotope-labeled analog of the product cleaved by a targeted enzyme upon the substrate.

The invention discloses a (R)-styrene glycol preparation method that utilizes site-directed mutagenesis to alter coenzyme specificity and stereoselectivity, belongs to the technical field of biocatalytic asymmetric transformation, and provides a recombinant Escherichia coli strain BL21 / pETSCR6768 with the preservation CCTCC NO of M208079, and an asymmetric transforming preparation method of (R)-styrene glycol. The preparation method leads Ser in position 67 and His in position 68 of a (S)-specific carbonyl reductase to mutate to Asp, constructs recombinant plasmid pETSCR6768, and feeds the Escherichia coli, thus obtaining the recombinant strain E.coli BL21 / pETSCR6768 which leads the coenzyme specificity of (S)-specific carbonyl reductase to change from NADPH to NADH; furthermore, the stereoselectivity of the product is altered from (S)-styrene glycol to (R)-styrene glycol, and the preparation method provides an effective way for preparing (R)-styrene glycol in high efficiency and low cost and has significant meaning for recognizing the stereoselectivity of functional zymoprotein in the molecule and protein level.