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95 results about "O-methyltransferase" patented technology

An O-methyltransferase (OMT) is a type of methyltransferase enzyme transferring a methyl group on a molecule.

Engineering bacteria for generating gentamicin C1a and constructing method of engineering bacteria

ActiveCN102586146AHigh C1a contentClear genetic backgroundBacteriaMicroorganism based processesMicromonospora echinosporaGentamicin C2b
The invention belongs to the technical field of medicines and relates to engineering bacteria for mainly generating gentamicin C1a and a constructing method of the engineering bacteria. 6'-C-O-methyltransferase gntK in micromonospora echinospora of gentamicin generated bacteria is damaged by using a gene blocking technology, so that the synthesis of gentamicin C1, C2 and C2a is blocked and gentamicin C1a and small part of gentamicin C2b are mainly generated. The contents of the C1A, the C2, the C2a and C1 in an original strain are 6.5 percent, 45.3 percent, 20.1 percent and 27.1 percent respectively; and the contents of the C1a and the C2b in a blocked strain are 94.0 percent and 6.0 percent respectively. According to the constructing method, the gntK gene in the micromonospora echinospora is damaged by a method of deleting in the architecture to inactivate, including the construction of gntK gene blocking plasmid, conversion of the blocking plasmid into the micromonospora echinospora, screening of a double-exchange strain and analysis of a fermentation product. The engineering bacteria constructed by the constructing method provided by the invention have no resistant marker; and through continuous passage, the yield of the gentamicin C1a is very stable.
Owner:SHENYANG PHARMA UNIVERSITY

Specific probe substrate of catechol-O-methyltransgerase and application thereof

The invention provides a specific probe substrate of catechol-O-methyltransgerase and application thereof. The specific probe substrate is a 7,8-dihydroxycoumarin compound and can be used for determination of activity of COMT enzyme in mammalian tissue and cells from different sources. The determination comprises the following concrete steps: selecting a coumarin compound having hydroxyl groups at positions 7 and 8 as a highly specific probe substrate; carrying out a COMT catalyzed reaction of the specific probe substrate in virtue of a COMT in-vitro incubation system; and determining the activity of COMT enzyme in each biological sample and each cell through quantitative detection of a product generation amount per unit time. The specific probe substrate can be used for quantitative evaluation of the activity of COMT enzyme in biological samples of different species and from different individual sources and quantitative determination of the activity of COMT enzyme in different-source-derived animal tissue cell culture fluids and prepared cell products, so assessment of capability of the important drug metablic enzyme COMT in disposition of drugs can be realized.
Owner:ZHANGJIAGANG IND TECH RES INST CO LTD DALIAN INST OF CHEM PHYSICS CHINESE ACADEMY OF SCI

Radix scutellariae flavone phenylpropanoidand and flavonoid O-methyltransferase gene and vector construction and application thereof

The invention provides a radix scutellariae flavone phenylpropanoidand and flavonoid O-methyltransferase gene. The radix scutellariae flavone phenylpropanoidand and flavonoid O-methyltransferase genecomprises at least one of SbPFOMT1, SbPFOMT2 and SbPFOMT5 genes, the gene sequence of the SbPFOMT1 is as shown in SEQID No.1, the gene sequence of the SbPFOMT2 is as shown in SEQID No.3, and the genesequence of the SbPFOMT5 is as shown in SEQID No.5; and a primer composition amplifying the gene, protein coded by the gene, a recombinant vector, a recombinant microorganism, a host cell, a transgenic cell line, transgenic plant tissue or a transgenic plant constructed by the gene, and an application of the recombinant vector, the recombinant microorganism, the host cell, the transgenic cell line, the transgenic plant tissue or the transgenic plant are provided. The methylation process of wogonin and similar flavonoid is analyzed, 3 flavone phenylpropanoidand and flavonoid O-methyltransferasegenes SbPFOMT1, SbPFOMT2 and SbPFOMT5 are obtained for the first time and cloned, besides, the function of enzymes coded by the gene is verified in an exogenous plant and a microorganism body, a theoretical basis is provided for methylation of wogonin and similar flavonoid in mass production, and a firm basis is also established for industrial production of other pertinent flavonoid compounds.
Owner:SHANGHAI CHENSHAN BOTANICAL GARDEN

Specific fluorescent probe for catechol-O-methyltransgerase (COMT) and application thereof

The invention provides a specific fluorescent probe for COMT and application thereof. A specific probe substrate provided by the invention is 3-benzothiazole-7,8-dihydroxycoumarin (3-BTD); the substrate can be specifically catalyzed by COMT to produce an 8-methoxy product and presents a fluorescence signal at a position of 520 nm; and the activity of COMT can be quantitatively determined by detecting changes of fluorescence intensity. The probe is applicable to quantitative assessment of the activity of COMT in biological samples from different sources, in-vitro rapid screening of inhibitors for COMT and evaluation of the inhibitory capability of the inhibitors. A method provided by the invention can be used for quantitative assessment of the actual activity of COMT in a variety of in-vitro biological samples and realizes rapid screening of inhibitors and quantitative assessment of the inhibitory capability of the inhibitors; the method is also applicable to evaluation of the catalytic activity of COMT of different species and COMT mutants with different amino acid sequences, so the method can assess the capability of COMT in metabolization of catechol drugs; and the method has the advantages of high sensitivity, high accuracy, good environment interference resisting capability, convenience in high-flux detection and inhibitor screening, etc.
Owner:DALIAN INST OF CHEM PHYSICS CHINESE ACAD OF SCI
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