Abstract: Compositions, devices, kits and methods are disclosed for assaying glucose with a glucose oxidase mutant that has been modified at an amino acid residue involved in the active site. The glucose oxidase mutant has reduced oxidase activity while substantially maintaining its dehydrogenase activity.

Abstract: The invention provides compounds and methods of their use in the detection of apoptosis and necrosis both in vitro and in vivo. Also provided are compounds and methods of their use in selective delivery of agents to cells undergoing apoptosis or necrosis. The compounds and methods are based on conjugates formed with a dehydrogenase such as lactate dehydrogenase, alcohol dehydrogenase, aldehyde dehydrogenase, and malate dehydrogenase. The compounds and methods are useful in the diagnosis and treatment of conditions characterized by apoptosis, including cancer, cardiac disease, neurologic disease including stroke, and autoimmunity. The compounds and methods offer distinct advantages over corresponding compounds and methods based on Annexin V. Also provided are methods for screening for compounds that modulate, i.e., inhibit or promote, apoptosis.

Abstract: The present invention relates to a modified cellobiose dehydrogenase (CDH) or its functional flavodehydrogenase domain having glucose oxidation activity and a reduced maltose oxidation activity as compared to the unmodified CDH or its functional flavodehydrogenase domain, nucleic acids encoding said enzyme or domain, electrodes with said enzyme or domain and methods of producing and using the same.

Abstract: The present disclosure provides engineered ketoreductase enzymes having improved properties as compared to a naturally occurring wild-type ketoreductase enzyme. Also provided are polynucleotides encoding the engineered ketoreductase enzymes, host cells capable of expressing the engineered ketoreductase enzymes, and methods of using the engineered ketoreductase enzymes to synthesize a variety of chiral compounds.

Abstract: The present disclosure provides engineered ketoreductase enzymes having improved properties as compared to a naturally occurring wild-type ketoreductase enzyme. Also provided are polynucleotides encoding the engineered ketoreductase enzymes, host cells capable of expressing the engineered ketoreductase enzymes, and methods of using the engineered ketoreductase enzymes to synthesize a variety of chiral compounds.

Abstract: The present invention concerns a method for the production of 1,2-propanediol, comprising culturing a microorganism modified for an improved production of 1,2-propanediol in an appropriate culture medium and recovery of the 1,2-propanediol which may be further purified wherein the microorganism expresses a glycerol dehydrogenase (GlyDH) enzyme the inhibition of which activity by NAD+ and/or its substrate and/or its product is reduced. The present invention also relates to a mutant glycerol dehydrogenase (GlyDH) comprising at least one amino acid residue in the protein sequence of the parent enzyme replaced by a different amino acid residue at the same position wherein the mutant enzyme has retained more than 50% of the glycerol dehydrogenase activity of the parent enzyme and the glycerol dehydrogenase activity of the mutant GlyDH is less inhibited by NAD+ and/or by its substrate as compared to the parent enzyme and/or by its product as compared to the parent enzyme.

Abstract: Methods for the fermentive production of four carbon alcohols are provided. Specifically, butanol, preferably 2-butanol is produced by the fermentive growth of a recombinant bacteria expressing a 2-butanol biosynthetic pathway. The recombinant microorganisms and methods of the invention can also be adapted to produce 2-butanone, an intermediate in the 2-butanol biosynthetic pathways disclosed herein.

Abstract: Compositions, devices, kits and methods are disclosed for assaying glucose with a glycosylated, modified flavin adenine dinucleotide-dependent glucose dehydrogenase (FAD-GDH), variant thereof or an active fragment thereof, where at least one asparagine residue at positions N2, N168 and N346 of mature, wild-type A. oryzae FAD-GDH according to SEQ ID NO:2 is substituted by one or more amino acids not suitable for glycosylation, thereby eliminating or inactivating, respectively, a potential glycosylation site at this position.

Abstract: Described herein are novel nucleic acids, proteins and methods that can be used to provide new catalysts with desirable traits for industrial processes. In particular, novel reductases isolated from the environment using PCR methods are described.

Abstract: The purpose of the present invention is to provide an FAD-conjugated glucose dehydrogenase that is hard to be inhibited by the inhibitors such as 1,10-phenanthroline. The present invention relates to a modified glucose dehydrogenase (GLD), comprising an amino acid sequence of a wild-type FAD-conjugated glucose dehydrogenase (GLD) represented by SEQ ID NO: 1 having a substitution of at least one amino acid residue selected from the group consisting of amino acid residues at positions 298, 338, 340, 341, 343, 352, 354, 424, 426, 431 and 432, wherein the modified GLD has a reduced susceptibility to an inhibitor, as compared with the wild-type GLD, especially to said modified GLD, which has 40% or more of a relative activity when determined in a system wherein the inhibitor coexists at a final concentration of 1 mM based on an enzymatic activity when determined in a system wherein the inhibitor does not coexist.

Abstract: Methods for the fermentive production of four carbon alcohols are provided. Specifically, butanol, preferably 2-butanol is produced by the fermentive growth of a recombinant bacteria expressing a 2-butanol biosynthetic pathway. The recombinant microorganisms and methods of the invention can also be adapted to produce 2-butanone, an intermediate in the 2-butanol biosynthetic pathways disclosed herein.

Abstract: The present disclosure provides engineered ketoreductase enzymes having improved properties as compared to a naturally occurring wild-type ketoreductase enzyme. Also provided are polynucleotides encoding the engineered ketoreductase enzymes, host cells capable of expressing the engineered ketoreductase enzymes, and methods of using the engineered ketoreductase enzymes to synthesize chiral compounds.

Abstract: The present disclosure provides engineered ketoreductase enzymes having improved properties as compared to a naturally occurring wild-type ketoreductase enzyme including the capability of reducing 5-((4S)-2-oxo-4-phenyl(1,3-oxazolidin-3-yl))-1-(4-fluorophenyl)pentane-1,5-dione to (4S)-3-[(5S)-5-(4-fluorophenyl)-5-hydroxypentanoyl]-4-phenyl-1,3-oxazolidin-2-one. Also provided are polynucleotides encoding the engineered ketoreductase enzymes, host cells capable of expressing the engineered ketoreductase enzymes, and methods of using the engineered ketoreductase enzymes to synthesize the intermediate (4S)-3-[(5S)-5-(4-fluorophenyl)-5-hydroxypentanoyl]-4-phenyl-1,3-oxazolidin-2-one in a process for making Ezetimibe.

Abstract: The biosynthesis of fungal bicyclo[2.2.2]diazaoctane indole alkaloids with a wide spectrum of biological activities have attracted increasing interest. Their intriguing mode of assembly has long been proposed to feature a non-ribosomal peptide synthetase, a presumed intramolecular Diels-Alderase, a variant number of prenyltransferases, and a series of oxidases responsible for the diverse tailoring modifications of their cyclodipeptide-based structural core. Until recently, the details of these biosynthetic pathways have remained largely unknown due to lack of information on the fungal derived biosynthetic gene clusters. Herein, we report a comparative analysis of four natural product metabolic systems of a select group of bicyclo[2.2.2]diazaoctane indole alkaloids including (+)/(?)-notoamide, paraherquamide and malbrancheamide, in which we propose an enzyme for each step in the biosynthetic pathway based on deep annotation and on-going biochemical studies.

Abstract: The object of the present invention is to provide a method of determining 1,5-anhydroglucitol, including using (a) a protein which consists of the amino acid sequence of SEQ ID NO: 2; (b) a protein which consists of an amino acid sequence having deletion, substitution and/or addition of one or more amino acid residues in the amino acid sequence of SEQ ID NO: 2 and which has sorbose dehydrogenase activity; or (c) a protein which consists of an amino acid sequence having a homology of at least 60% with the amino acid sequence of SEQ ID NO: 2 and which has sorbose dehydrogenase activity.

Abstract: The invention provides a flavin-binding glucose dehydrogenase exhibiting reduced fluctuation of activity depending on temperature environment, and a method for measuring glucose concentration using the flavin-binding glucose dehydrogenase. The flavin-binding glucose dehydrogenase has the following properties (1) to (3): (1) activity: which exhibits glucose dehydrogenase activity in the presence of an electron acceptor; (2) substrate specificity: which exhibits an activity of 10% or less against maltose, D-galactose, D-fructose, sorbitol, lactose and sucrose when the activity against D-glucose is defined as 100%; and (3) temperature characteristics: which exhibits lower fluctuation of activity in a wide temperature range of 10 to 50° C.

Abstract: The present disclosure provides engineered ketoreductase enzymes having improved properties as compared to a naturally occurring wild-type ketoreductase enzyme. Also provided are polynucleotides encoding the engineered ketoreductase enzymes, host cells capable of expressing the engineered ketoreductase enzymes, and methods of using the engineered ketoreductase enzymes to synthesize a variety of chiral compounds. The engineered ketoreductase polypeptides are optimized for catalyzing the conversion of N-methyl-3-keto-3-(2-thienyl)-1-propanamine to (S)—N-methyl-3-hydroxy-3-(2-thienyl)-1-propanamine.

Abstract: The present invention provides compositions and methods for producing a polyol oxidase in micoroorganisms, and the use of polyol oxidases in cleaning compositions. The invention includes cleaning compositions that contain combinations of two or more POx oxidases, and cleaning compositions that contain combinations of two or more POx oxidases and a perhydrolase. In particular, the invention provides methods for expressing polyol oxidases in bacterial hosts for use in detergent applications for cleaning, bleaching and disinfecting.

Abstract: An object of the present invention is to provide a novel glucose dehydrogenase, a method for producing the glucose dehydrogenase, and applications of the glucose dehydrogenase. The flavin-binding glucose dehydrogenase of the invention has the following characteristics (1) and (4): (1) Molecular weight: the molecular weight of a polypeptide moiety in the enzyme is about 68 kDa as measured by SDS-polyacrylamide electrophoresis; (2) Km value: the Km value for D-glucose is about 15 mM or less; (3) Temperature stability: stable at a temperature of 55° C. or less; and (4) pH stability: stable at a pH range of 3.0 to 8.5.

Abstract: An object is to provide a novel enzyme that exhibits glucose dehydrogenase activity. Furthermore, another object is to provide a novel method pertaining to enzyme modification. Provided is a mutated enzyme containing an amino acid sequence wherein one or at least two amino acids selected from a group are substituted with another amino acid in the amino acid sequence of a microorganism-derived glucose oxidase.

Abstract: A mutant butyraldehyde dehydrogenase (Bld), a polynucleotide having a nucleotide encoding the mutant, a vector including the polynucleotide, a microorganism including a nucleotide encoding the mutant, and a method of producing 1,4-butanediol using the same.

Abstract: A process for the enantioselective enzymatic reduction of a keto compound of general formula I wherein R may represent any protective group for amino functions (tert. butyloxycarbonyl group (BOC), benzyloxycarbonyl group, 9-fluorenylmethoxycarbonyl group) and X?—Cl, —CN, —OH, Br, F.

Abstract: The present invention relates to a composition for forming an electrode, an electrochemical sensor comprising the same, and a method for determining an analyte using the electrochemical sensor.

Abstract: The disclosure relates to a nucleic acid molecule isolated from a Papaver somniferum cultivar that produces the opiate alkaloid noscapine which comprises 10 genes involved in the biosynthesis of opiate alkaloids.

Abstract: This patent application discloses and describes proteins found to be differentially expressed between primary tumor breast cancer cells histologicaly defined as early stage (stage 0) breast cancer and primary breast cancer cells histologicaly defined as late stage (stage 3) breast cancer. These proteins can be used either individually or in specific combinations in diagnostic and prognostic protein assays on various biological samples from breast cancer patients to indicate the that a breast cancer patient's cancer is in an early, non-aggressive stage or in a late, aggressive stage. Determination of differential expression of these proteins can also be useful for indicating additional therapies to combat the aggressiveness of late stage breast cancer. The full length intact proteins can be assayed or peptides derived from these proteins can be assayed as reporters for these proteins.

Abstract: A method for the secretory production of a glycoprotein having a human-type sugar chain, comprising a step of introducing a gene of an enzyme capable of performing a transfer reaction of a galactose residue to a non-reducing terminal acetylglucosamine residue, and a gene of heterologous glycoprotein, to obtain a transformed plant cell, a step of culturing the plant cell, and a step of recovering the culture medium of the plant cell.

Abstract: The present invention is to enhance the stability and enzyme activity of an L-arabitol dehydrogenase derived from Neurospora crassa using techniques from quantum mechanics and molecular mechanics and partial mutation techniques. More specifically, the present invention relates to a method for preparing an L-arabitol dehydrogenase in which a residue which affects enzyme stability is found through a screening based on quantum mechanics and molecular mechanics, and enzyme activity is enhanced by mutation of the found residue, nucleic acid molecules encoding the L-arabitol dehydrogenase, a vector including the nucleic acid molecules, a transformant including the vector, a mutant of the L-arabitol dehydrogenase and an improved L-arabitol dehydrogenase.

Abstract: The invention provides non-naturally occurring microbial organisms having a 4-hydroxybutyrate, gamma-butyrolactone, 1,4-butanediol, 4-hydroxybutanal, 4-hydroxybutyryl-CoA and/or putrescine pathway and being capable of producing 4-hydroxybutyrate, wherein the microbial organism comprises one or more genetic modifications. The invention additionally provides methods of producing 4-hydroxybutyrate, gamma-butyrolactone, 1,4-butanediol, 4-hydroxybutanal, 4-hydroxybutyryl-CoA and/or putrescine or related products using the microbial organisms.

Abstract: A method of increasing cellular NADPH levels by expressing one or more genes that encode an enzyme that causes the production of NADPH. The system is combined with other enzymes that require NADPH, thus improving the overall yield of the desired product.

Abstract: Amino acid mutation(s) can be introduced to Sclerotinia sclerotiorum- or Aspergillus niger-derived glucose dehydrogenase to obtain a glucose dehydrogenase variant with significantly enhanced productivity in E. coli. The glucose dehydrogenase of the present invention is low reactive with xylose.

Abstract: Disclosed herein are various open reading frames from a strain of E. coli responsible for neonatal meningitis (MNEC), and a subset of these that is of particular interest for preparing compositions for immunising against MNEC infections.

Abstract: A microorganism genetically modified for the bioproduction of 1,3-propanediol from sucrose, wherein the microorganism includes: a two-step metabolic pathway for the production of 1,3-propanediol, including a first step of decarboxylation of 4-hydroxy-2-ketobutyrate with an enzyme having a 2-keto acid decarboxylase activity, and a second step of reduction of the obtained 3-hydroxypropionaldehyde with an enzyme having hydroxy aldehyde reductase activity, and genes enabling the microorganism to utilize sucrose as sole carbon source. A method for the biological preparation of 1,3-propanediol by fermentation, including cultivating said microorganism genetically modified, wherein the culture is performed in an appropriate medium including a source of sucrose, and recovering the 1,3-propanediol being produced.

Abstract: An expression vector is provided. The vector includes a promoter configured to drive the expression of the transgene in the cell. The vector also includes a tag sequence encoding a tag peptide directing the protein of the expressed transgene to a pre-determined location. The vector further includes a cleavage sequence encoding a peptide that is recognizable by a protease and a marker gene configured to encoding a protein to indicate the expression of the transgene.

Abstract: A method for treatment and/or prevention of common cold caused by rhinovirus, wherein a patient in need is treated with a medicament including a hydrogen peroxide producing enzyme.

Abstract: Disclosed are polynucleotides encoding polypeptides that comprise the biosynthetic pathway for lignin in the jute plant. The present invention relates generally to the field of plant lignin biosynthesis genes, polypeptides encoded by such genes, and the use of such polynucleotide and polypeptide sequences for controlling plant lignin production. Also disclosed are methods for using the polynucleotides and polypeptides to influence the quality and amount of fiber produced by jute.

Abstract: An object is to provide a novel enzyme that exhibits glucose dehydrogenase activity. Furthermore, another object is to provide a novel method pertaining to enzyme modification.

Abstract: The present disclosure provides engineered ketoreductase enzymes having improved properties as compared to a naturally occurring wild-type ketoreductase enzyme. Also provided are polynucleotides encoding the engineered ketoreductase enzymes, host cells capable of expressing the engineered ketoreductase enzymes, and methods of using the engineered ketoreductase enzymes to synthesize a variety of chiral compounds. The engineered ketoreductase polypeptides are optimized for catalyzing the conversion of N-methyl-3-keto-3-(2-thienyl)-1-propanamine to (S)—N-methyl-3-hydroxy-3-(2-thienyl)-1-propanamine.

Abstract: The present disclosure relates to engineered ketoreductase polypeptides for the preparation of hydroxyl substituted carbamate compounds, and polynucleotides, vectors, host cells, and methods of making and using the ketoreductase polypeptides.

Abstract: It is intended to provide a novel NAD+-independent myo-inositol 2-dehydrogenase which converts myo-inositol into scyllo-inosose in the absence of NAD+; a novel enzyme scyllo-inositol dehydrogenase which stereospecifically reduces scyllo-inosose into scyllo-inositol in the presence of NADH or NADPH; and a novel microorganism which belongs to the genus Acetobacter or Burkholderia and can convert myo-inositol into scyllo-inositol. By using these enzymes or the microorganism, scyllo-inositol is produced. Furthermore, scyllo-inositol is purified by adding boric acid and a metal salt to a liquid mixture containing scyllo-inositol and a neutral saccharide other than scyllo-inositol to form a scyllo-inositol/boric acid complex, separating the complex from the liquid mixture, dissolving the thus separated complex in an acid to give an acidic solution or an acidic suspension and then purifying scyllo-inositol from the acidic solution or the acidic suspension.

Abstract: The present invention relates to mutants of the Penicillium amagasakiense glucose oxidase (GOx) enzyme which are of use for assaying glucose and to the development in particular of glucose electrodes and of biocells which use glucose as fuel.

Abstract: Provided is a novel method for preparing metabolites of atorvastatin using bacterial cytochrome P450, and a composition therefor, and more particularly, a composition for preparing 2-hydroxylated product of 4-hydroxylated product from atorvastatin including bacterial cytochrome P 450 BM3 (CYP102A1), CYP102A1 mutants, and chimeras derived from the CYP102A1 mutants, a kit therefor, and a method for preparing thereof.

Abstract: An object to be attained by the present invention is to provide a method for conveniently, rapidly, and specifically measuring HDL-C in a specimen by use of inexpensive materials, and to provide a reagent kit for HDL-C detection and a dry analytical element for HDL-C detection. The present invention provides a method for measuring high density lipoprotein cholesterol (HDL-C) in a body fluid test sample, wherein cholesterol esterase derived from Schizophyllum commune or Pseudomonas sp. and cholesterol oxidase derived from Pseudomonas sp. are used to generate hydrogen peroxide from HDL-C, and thereby HDL-C is selectively measured.

Abstract: A flavin-binding glucose dehydrogenase having high substrate specificity for D-glucose and decreased reactivity to D-xylose and/or maltose. More specifically, a flavin-binding glucose dehydrogenase having one or more amino acid substitutions at a position corresponding to position 78, position 79, position 81, position 121, position 122, position 123, position 569 and position 612 of Mucor-derived flavin-binding glucose dehydrogenase. The flavin-binding glucose dehydrogenase enables D-glucose to be measured accurately without being susceptible to the effects of the presence of D-xylose and/or maltose, even under conditions of mounting a large amount of an enzyme such as in glucose sensors.

Abstract: A novel polyol oxidase is derived from a microorganism belonging to the genus Penicillium and is specified by the properties (a) to (e): (a) it has a stable pH of 6.0 or higher and an optimum reaction pH of from 7.0 to 9.0; (b) it has an operating temperature of 50° C. or lower and an optimum reaction temperature of 40° C.; (c) it has a molecular weight of about 113 kDa; (d) it specifically recognizes the structure of a polyol in which the OH groups at positions 2 and 3 are in the L-erythro configuration and reacts with the polyol, but cannot recognize the structure of a polyol in which the OH group at position 4 is in the L-ribo configuration and does not react with the polyol; and (e) it has substrate specificity for D-arabitol, erythritol, D-mannitol, and D-sorbitol, which are listed in descending order of specificity.

Abstract: The present invention refers to the gene cluster and genes comprised by the gene cluster which are involved in the biosynthesis of griselimycin and methylgriselimycin and to the use of the gene cluster, genes comprised thereby and proteins encoded thereby for the production of antibiotic agents.

Abstract: The present invention relates to isolated polypeptides having protease activity and isolated polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods for producing and using the polypeptides.

Abstract: The present invention relates to recombinant microorganisms comprising at least one nucleic acid molecule encoding a ketol-acid reductoisomerase (KARI) or modified NADH-dependent variant thereof, wherein said KARI is at least about 60% identical to SEQ ID NO: 2. In various aspects of the invention, the recombinant microorganisms may comprise an isobutanol producing metabolic pathway and can be used in methods of making isobutanol.

Abstract: The present invention relates to recombinant microorganisms comprising at least one nucleic acid molecule encoding a ketol-acid reductoisomerase (KARI) or a modified NADH-dependent variant thereof, wherein said KARI is at least about 80% identical to SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 10, SEQ ID NO: 28, SEQ ID NO: 40, or SEQ ID NO: 58. The present invention also relates to recombinant microorganisms comprising at least one nucleic acid molecule encoding a ketol-acid reductoisomerase (KARI) or a modified NADH-dependent variant thereof, wherein said KARI is at least about 99% identical to SEQ ID NO: 64. In various aspects of the invention, the recombinant microorganisms may comprise an isobutanol producing metabolic pathway and can be used in methods of making isobutanol.

Abstract: In a step of contacting an organic material including formic acid ions and a carbon source other than the formic acid ions with a microorganism having a formate dehydrogenase gene and a hydrogenase gene under an anaerobic condition, concentration of the formic acid ions in the organic material is set to be not less than 0.01 mol/L and not more than 0.5 mol/L, and concentration of the carbon source is set to not less than 0.1 mmol/L and not more than 200 mmol/L. This allows continuously producing hydrogen for a long time, without dropping the ability of the microorganism to produce hydrogen.

Abstract: A flavin-binding glucose dehydrogenase (FAD-GDH), which in addition to having high substrate specificity and adequate desirable heat stability, is suitable for efficient production, preferably using E. coli, yeast or molds and the like as host cells. The FAD-GDH has amino acid substitutions at positions equivalent to one or more locations selected from the group consisting of position 213, position 368 and position 526 in the amino acid sequence described in SEQ ID NO: 8. The FAD-GDH is acquired from a culture by inserting a gene encoding the FAD-GDH into host cells such as E. coli. A preferable example of the FAD-GDH is FAD-GDH, in which a signal peptide region present in an N-terminal region has been deleted from the amino acid sequence of Mucor-derived FAD-GDH, and which has the aforementioned amino acid substitutions. The FAD-GDH can be preferably used in clinical diagnosis.