Abstract: A novel enzyme which has an activity to release side chain carboxyl groups and ammonia from a protein by acting upon side chain amido groups in the protein. This invention relates to a method for the production of an enzyme, which comprises culturing in a medium a strain that belongs to a bacterium classified into Cytophagales or Actinomiycetes and has the ability to produce an enzyme having a property to deamidate amido groups in protein, thereby effecting production of said enzyme, and subsequently collecting said enzyme from the culture mixture. It also relates to a method for the modification of protein making use of a novel enzyme which directly acts upon amido groups in protein as well as to an enzyme which has a property to deamidate amido groups in protein and a gene which encodes said enzyme.

Abstract: The invention provides methods for stabilizing recombinant Helicobacter urease by genetically modifying a urease amino acid. The stabilized urease is prevented from the molecular aggregation or activation (e.g., in vitro activation) characteristic of untreated urease.

Abstract: The present invention provides a vector containing a DNA construct containing a first promoter that is a nitrilase gene promoter, a multicloning site and a nitrilase transcription regulatory protein gene (particularly preferably a structural gene is ligated into a multicloning site and a second promoter is placed at the upstream of the nitrilase transcription regulatory protein gene), and the like. The present invention affords a high expression system capable of expressing a large amount of useful proteins by actinomycete host represented by actinomycete belonging to the genus Streptomyces and the like beneficially used for the production of useful proteins.

Abstract: Reagents which regulate human histone deacetylase and reagents which bind to human histone deacetylase gene products can play a role in preventing, ameliorating, or correcting dysfunctions or diseases including, but not limited to, cancer.

Abstract: The present invention provides materials and methods for the production of bifunctional enzymes that catalyze the N-deacetylation and N-sulfation of saccharides. The invention also provides conditions and methods for assaying the activity of such enzymes.

Abstract: The soporific activity of cis-9,10-octadecenoamide and other soporific fatty acid primary amides is neutralized by hydrolysis in the presence of fatty-acid amide hydrolase (FAAH). Hydrolysis of cis-9,10-octadecenoamide by FAAH leads to the formation of oleic acid, a compound without soporific activity. FAAH has be isolated and the gene encoding FAAH has been cloned, sequenced, and used to express recombinant FAAH. Inhibitors of FAAH are disclosed to block the hydrolase activity.

Abstract: This invention provides amidases, polynucleotides encoding the amidases, methods of making and using these polynucleotides and polypeptides. In one aspect, the invention provides enzymes having secondary amidase activity, e.g., having activity in the hydrolysis of amides, including enzymes having peptidase, protease and/or hydantoinase activity. In alternative aspects, the enzymes of the invention can be used to used to increase flavor in food (e.g., enzyme ripened cheese), promote bacterial and fungal killing, modify and de-protect fine chemical intermediates, synthesize peptide bonds, carry out chiral resolutions, hydrolyze Cephalosporin C. The enzymes of the invention can be used to generate 7-aminocephalosporanic acid (7-ACA) and semi-synthetic cephalosporin antibiotics, including caphalothin, cephaloridine and cefuroxime. The enzymes of the invention can be used as antimicrobial agents, e.g., as cell wall hydrolytic agents.

Abstract: The invention relates to nitrilases and to nucleic acids encoding the nitrilases. In addition methods of designing new nitrilases and method of use thereof are also provided. The nitrilases have increased activity and stability at increased pH and temperature.

Abstract: The present invention discloses novel amdS genes from fungi previously not known to contain and amdS gene, such as Aspergillus niger and Penicillium chrysogenum. The novel amdS genes can be used as homologous selectable marker genes in the transformation of these fungi. Alternatively, the cloned amdS genes can be used to inactivate the endogenous copy of the gene in order to reduce the background in transformation experiments.

Abstract: The present invention is related to a conjugate of a hapten to a natural or synthetic &bgr;-lactam derivative, comprising at least a side chain, wherein the side chain of the &bgr;-lactam derivative is at least partially constitutive of the conjugating arm.

Abstract: The present invention provides a family of bacterial acyl glucosaminylinositol amidases with amidase activity against S-conjugate amides, particularly mycothiol-derived S-conjugate amides. The invention amidases are characterized by a highly conserved 20 amino acid N-terminal region and four highly conserved histidine-containing regions and by having amidase activity, particularly amide hydrolase activity. The invention further provides methods for using the invention amidases in drug screening assays to determine compounds with antibiotic activity or compounds that inhibit activity or production of endogenous acyl glucosaminyl inositol amidase in bacteria. The invention further provides methods for detoxifying a toxic substance by contacting the toxic substance with an invention amidase, for example, by expression of the amidase under environmental conditions in a bacterium.

Abstract: The present invention relates to a process for delaying the deactivation of glutaryl amidase during enzyme catalysis. The enzyme catalyst is, after maximum conversion of the substrate, separated off by filtration and can be reused in a subsequent reaction batch. In each reaction cycle, the enzyme catalyst loses activity. The inactivation of the enzyme catalyst can be delayed by bringing it into contact with a thiol during the reaction.

Abstract: This invention provides a novel D-aminoacylase obtained by cloning a DNA encoding the novel D-aminoacylase from Methylobacterium mesophilicum MT 10894, etc. and which shows sufficiently high activity at an industrially useful substrate concentration to allow a D-amino acid to be efficiently produced from an N-acyl-DL-amino acid; a DNA encoding the D-aminoacylase; a process for producing a D-amino acid from the corresponding N-acylamino acid using a transformant containing the DNA.

Abstract: The present invention provides a novel D-aminoacylase, as well as method for producing a D-amino acid using the same. In order to achieve the above objective , the present inventors have succeeded in purifying heat-stable D-aminoacylase from microorganisms belonging to the genus Streptomyces by combining various purification methods. Furthermore, the present inventors found that the purified heat-stable D-aminoacylase is useful in industrial production of D-amino acids. By utilizing the heat-stable D-aminoacylase, it is possible to readily and efficiently produce the corresponding D-amino acids from N-acetyl-DL-amino acids (for example, N-acetyl-DL-methionine, N-acetyl-DL-valine, N-acetyl-DL-tryptophan, N-acetyl-DL-phenylalanine, N-acetyl-DL-alanine, N-acetyl-DL-leucine, and so on).

Abstract: The present invention relates to an amidase enzyme, nucleic acids encoding the amidase, as well as methods of employing the nucleic acids and/or amidase to produce, for example, enantiomericallyenriched compounds such as D-amino acids.

Abstract: This invention relates to methods for the stabilization, storage and delivery of biologically active macromolecules, such as proteins, peptides and nucleic acids. In particular, this invention relates to protein or nucleic acid crystals, formulations and compositions comprising them. Methods are provided for the crystallization of proteins and nucleic acids and for the preparation of stabilized protein or nucleic acid crystals for use in dry or slurry formulations. The present invention is further directed to encapsulating proteins, glycoproteins, enzymes, antibodies, hormones and peptide crystals or crystal formulations into compositions for biological delivery to humans and animals. According to this invention, protein crystals or crystal formulations are encapsulated within a matrix comprising a polymeric carrier to form a composition.

Abstract: A whole cell catalyst is described comprising a hydantoinase, a racemase and a carbamoylase. Thus this catalyst is able to degrade hydantoins directly into the amino acids.

Abstract: D-aminoacylase derived from fungi is provided. The fungi capable of producing D-aminoacylase include those belonging to the genus Hypomyces, Fusarium, Auricularia, Pythium, and Menisporopsis. The fungal D-aminoacylase is useful for efficiently producing D-amino acids from N-acetyl-D-amino acids.

Abstract: Staphylococcus aureus peptide deformylase has been crystallized, and the three-dimensional x-ray crystal structure has been solved to 1.9 Å resolution. The x-ray crystal structure is useful for solving the structure of other molecules or molecular complexes, and designing modifiers of peptide deformylase activity.

Abstract: The invention relates to the synthesis of aspartame involving enzymatic deformylation of an N-formyl-&agr;-L-aspartyl-L-phenylalanine compound by treatment with an enzyme having formylmethionyl peptide deformylase activity and having as a co-factor group 5 to 11 bivalent metal ions. The invention also relates to selective preparation and recovery of aspartame from a mixture of N-formyl-&agr;- and &bgr;-L-aspartyl-L-phenylalanine compounds by treatment with such enzyme. And finally, the invention relates to one-pot enzymatic synthesis of aspartame from N-formyl-L-aspartic acid and L- or D,L-phenylalanine methyl ester involving an enzymatic deformylation reaction simultaneously with an enzymatic coupling reaction, as well as to one-pot di- or oligopeptide synthesis by simultaneous enzymatic coupling and deformylation reactions in general.

Abstract: The present invention relates to a novel protein having amidase activity that stereoselectively hydrolyzes &agr;-amino acid amides and &agr;-hydroxy acid amides, and a gene encoding said protein.

Abstract: Recombinant microbial strains are provided that express nitrilase enzyme and are useful as biocatalysts for the hydrolysis of nitrile-containing substrates. The recombinant cells are transformed with a foreign gene isolated from Acidovorax facilis 72W encoding a thermostable nitrilase enzyme that catalyzes the hydrolysis of nitrile-containing substrates to carboxylic acids under mild reaction conditions. The nucleotide sequence of the nitrilase gene and the deduced amino acid sequence encoded by the nitrilase gene are provided.

Abstract: The present invention relates to a novel sphingolipid ceramide N-deacylase (SCDase) having a wide substrate specificity; a method for enzymatically producing a lysosphingolipid or a sphingolipid derivative using the SCDase which is useful in the fields of medicine, carbohydrate engineering, cell engineering, and the like; the lysosphingolipid or sphingolipid derivative obtained by this production method; a gene which encodes a polypeptide having an SCDase activity useful in sphingolipid technology; a method for industrially producing a polypeptide having an SCDase deacylase activity and a recombinant polypeptide thereof using a transformant to which the gene is introduced; a probe or primer which hybridizes to the gene; and an antibody or a fragment thereof which specifically binds to the polypeptide.

Abstract: One or more biocatalysts or a combinatorial array of biocatyalysts is produced by providing a host cell; recombining at least two biotransformation genes for modifying a chemical substrate into the host cell; and thereby producing at least one recombinant strain comprising a biocatalysts. Additionally, the screening of cells having at least two distinct biotransforming catalysts combined therein may be performed by providing multiple wells, each of the multiple wells containing cells having at least two distinct biotransforming catalysts combined therein; and providing multiple wells, each of the wells containing different cells having at least two distinct biotransforming catalysts combined therein; and then allowing cells within the well to catalyze a reaction with a compound within each well, and analyzing the results of any reactions within each well to determine any functional activity of cells within each well.

Abstract: The present invention provides a novel D-aminoacylase, as well as method for producing a D-amino acid using the same. In order to achieve the above objective, the present inventors have succeeded in purifying heat-stable D-aminoacylase from microorganisms belonging to the genus Streptomyces by combining various purification methods. Furthermore, the present inventors found that the purified heat-stable D-aminoacylase is useful in industrial production of D-amino acids. By utilizing the heat-stable D-aminoacylase, it is possible to readily and efficiently produce the corresponding D-amino acids from N-acetyl-DL-amino acids (for example, N-acetyl-DL-methionine, N-acetyl-DL-valine, N-acetyl-DL-tryptophan, N-acetyl-DL-phenylalanine, N-acetyl-DL-alanine, N-acetyl-DL-leucine, and so on).

Abstract: Capsaicin decomposing/synthesizing enzymes are disclosed, which each have the following physical and chemical properties: (1) function and substrate specificity: the enzyme catalyzes a decomposition and/or synthesis reaction of capsaicin and/or capsaicin analogs; (2) an optimal temperature range: near 55° C.; and(3) an optimal pH range of 7-8. Microorganisms to be used for producing these enzymes are also disclosed.

Abstract: The invention provides a glutaryl 7-ACA amidase from Pseudomonas diminuta strain BS-203, which catalyzes the hydrolysis of 7-&bgr;-(4-carboxybutanamido)-cephalosporanic acid to 7-aminocephalosporanic acid and glutaric acid. The invention also provides nucleic acid sequences, vectors, and host cells useful in the production of this amidase. The glutaryl 7-ACA amidase can be used for the preparation of 7-aminocephalosporanic acid.

Abstract: The present invention provides a novel D-aminoacylase, as well as method for producing a D-amino acid using the same. In order to achieve the above objective, the present inventors have succeeded in purifying heat-stable D-aminoacylase from microorganisms belonging to the genus Streptomyces by combining various purification methods. Furthermore, the present inventors found that the purified heat-stable D-aminoacylase is useful in industrial production of D-amino acids. By utilizing the heat-stable D-aminoacylase, it is possible to readily and efficiently produce the corresponding D-amino acids from N-acetyl-DL-amino acids (for example, N-acetyl-DL-methionine, N-acetyl-DL-valine, N-acetyl-DL-tryptophan, N-acetyl-DL-phenylalanine, N-acetyl-DL-alanine, N-acetyl-DL-leucine, and so on).

Abstract: This invention is directed to a DNA sequence encoding a pepper fibrillin gene promoter useful for driving expression of foreign genes in transgenic plants, and to plants comprised of the same.

Abstract: The present invention discloses novel amdS genes from fungi previously not known to contain and amdS gene, such as Aspergillus niger and Penicillium chrysogenum. The novel amdS genes can be used as homologous selectable marker genes in the transformation of these fungi. Alternatively, the cloned amdS genes can be used to inactivate the endogenous copy of the gene in order to reduce the background in transformation experiments.

Abstract: D-aminoacylase derived from fungi is provided. The fungi capable of producing D-aminoacylase include those belonging to the genus Hypomyces, Fusarium, Auricularia, Pythium, and Menisporopsis. The fungal D-aminoacylase is useful for efficiently producing D-amino acids from N-acetyl-D-amino acids.

Abstract: The present invention relates to a novel process for the preparation of (S)- or (R)-3,3,3-trifluoro-2-hydroxy-2-methylpropionic acid and to novel microorganisms capable of utilizing the propionamide of the formula 1

Abstract: The present invention discloses novel amdS genes from fungi previously not known to contain an amdS gene, such as Aspergillus niger and Penicllium chrysogenum. The novel amdS genes can be used as homologous selectable marker genes in the transformation of these fungi. Alternatively, the cloned amdS genes can be used to inactivate the endogenous copy of the gene in order to reduce the background in transformation experiments.

Abstract: New fumonisin detoxifying or fumonisin-derivative detoxifying homologues (both nucleic acids and proteins) are provided. Compositions which include these new proteins, recombinant cells, antibodies to the new homologues, and methods of using the homologues are also provided.

Abstract: The present invention is concerned with new micro organisms, preferably mutagenised, belonging to the genus Agrobacterium radiobacter able to convert nitriles and/or amides into their respective acids, in addition to conversion processes utilising said micro-organisms.

Abstract: The invention provides a glutaryl 7-ACA amidase from Pseudomonas diminuta strain BS-203, which catalyzes the hydrolysis of 7-&bgr;-(4-carboxybutanamido)-cephalosporanic acid to 7-aminocephalosporanic acid and glutaric acid. The invention also provides nucleic acid sequences, vectors, and host cells useful in the production of this amidase. The glutaryl 7-ACA amidase can be used for the preparation of 7-aminocephalosporanic acid.

Abstract: A purified thermostable enzyme is derived from the archael bacterium Thermococcus GU5L5. The enzyme has a molecular weight of about 68.5 kilodaltons and has cellulase activity. The enzyme can be produced from native or recombinant host cells and can be used for the removal of arginine, phenylalanine, or methionine amino acids from the N-terminal end of peptides in peptide or peptidomimetic synthesis. The enzyme is selective for the L, or ‘natural’ enantiomer of the amino acid derivatives and is therefore useful for the production of optically active compounds. These reactions can be performed in the presence of the chemically more reactive ester functionality, a step which is very difficult to achieve with nonenzymatic methods.

Abstract: A purified thermostable enzyme is derived from the archael bacterium Thermococcus GU5L5. The enzyme has a molecular weight of about 68.5 kilodaltons and has cellulase activity. The enzyme can be produced from native or recombinant host cells and can be used for the removal of arginine, phenylalanine, or methionine amino acids from the N-terminal end of peptides in peptide or peptidomimetic synthesis. The enzyme is selective for the L, or ‘natural’ enantiomer of the amino acid derivatives and is therefore useful for the production of optically active compounds. These reactions can be performed in the presence of the chemically more reactive ester functionally, a step which is very difficult to achieve with nonenzymatic methods.

Abstract: The soporific activity of cis-9,10-octadecenoamide and other soporific fatty acid primary amides is neutralized by hydrolysis in the presence of fatty-acid amide hydrolase (FAAH). Hydrolysis of cis-9,10-octadecenoamide by FAAH leads to the formation of oleic acid, a compound without soporific activity. FAAH has be isolated and the gene encoding FAAH has been cloned, sequenced, and used to express recombinant FAAH. Inhibitors of FAAH are disclosed to block the hydrolase activity.

Abstract: The invention provides isolated nucleic acids molecules, designated 32144 nucleic acid molecules, which encode novel fatty acid amide hydrolase members. The invention also provides antisense nucleic acid molecules, recombinant expression vectors containing 32144 nucleic acid molecules, host cells into which the expression vectors have been introduced, and nonhuman transgenic animals in which a 32144 gene has been introduced or disrupted. The invention still further provides isolated 32144 proteins, fusion proteins, antigenic peptides and anti-32144 antibodies. Diagnostic methods utilizing compositions of the invention are also provided.

Abstract: The invention provides a glutaryl 7-ACA amidase from Pseudomonas diminuta strain BS-203, which catalyzes the hydrolysis of 7-&bgr;-(4-carboxybutanamido)-cephalosporanic acid to 7-aminocephalosporanic acid and glutaric acid. The invention also provides nucleic acid sequences, vectors, and host cells useful in the production of this amidase. The glutaryl 7-ACA amidase can be used for the preparation of 7-aminocephalosporanic acid.

Abstract: A purified thermostable enzyme is derived from the archael bacterium Thermococcus GU5L5. The enzyme has a molecular weight of about 68.5 kilodaltons and has cellulase activity. The enzyme can be produced from native or recombinant host cells and can be used for the removal of arginine, phenylalanine, or methionine amino acids from the N-terminal end of peptides in peptide or peptidomimetic synthesis. The enzyme is selective for the L, or ‘natural’ enantiomer of the amino acid derivatives and is therefore useful for the production of optically active compounds. These reactions can be performed in the presence of the chemically more reactive ester functionally, a step which is very difficult to achieve with nonenzymatic methods.

Abstract: The invention relates to amidases and to polynucleotides encoding the amidases. In addition methods of designing new amidases and method of use thereof are also provided. The amidases have increased activity and stability at increased pH and temperature.

Abstract: Disclosed are polypeptides which originate from mammal, having L-asparaginase activity. The polypeptides are easily prepared by applying recombinant DNA techniques to DNAs encoding the polypeptides and they exert satisfactory effects in the treatment and/or the prevention for diseases caused by tumor cells dependent on L-asparagine, and cause no substantial serious side effects even when administered to humans in relatively-high dose.

Abstract: There are disclosed a protein having an amino acid sequence represented by amino acid numbers 1 to 684 or 49 to 684 shown in SEQ ID NO:2, or a protein having a glutaminase activity in which one or more amino acids is/are deleted from, substituted by, inserted to or added to the amino acid sequence of the above protein; a gene containing DNA encoding the above protein or a gene encoding a protein which hybridizes with the DNA of the above gene under a stringent condition and has a glutaminase activity; a recombinant DNA containing the above gene; a transformant or a transductant containing the above recombinant DNA; and a process for producing glutaminase which comprises culturing the above transformant or the above transductant and collecting glutaminase from a culture medium.

Abstract: The present invention relates to a novel sphingolipid ceramide N-deacylase (SCDase) having a wide substrate specificity; a method for enzymatically producing a lysosphingolipid or a sphingolipid derivative using the SCDase which is useful in the fields of medicine, carbohydrate engineering, cell engineering, and the like; the lysosphingolipid or sphingolipid derivative obtained by this production method; a gene which encodes a polypeptide having an SCDase activity useful in sphingolipid technology; a method for industrially producing a polypeptide having an SCDase deacylase activity and a recombinant polypeptide thereof using a transformant to which the gene is introduced; a probe or primer which hybridizes to the gene; and an antibody or a fragment thereof which specifically binds to the polypeptide.

Abstract: A purified thermostable enzyme is derived from the archael bacterium Thermococcus GU5L5. The enzyme has a molecular weight of about 68.5 kilodaltons and has cellulase activity. The enzyme can be produced from native or recombinant host cells and can be used for the removal of arginine, phenylalanine, or methionine amino acids from the N-terminal end of peptides in peptide or peptidomimetic synthesis. The enzyme is selective for the L, or ‘natural’ enantiomer of the amino acid derivatives and is therefore useful for the production of optically active compounds. These reactions can be performed in the presence of the chemically more reactive ester functionally, a step which is very difficult to achieve with nonenzymatic methods.

Abstract: The present invention provides a novel D-aminoacylase, as well as method for producing a D-amino acid using the same. In order to achieve the above objective, the present inventors have succeeded in purifying heat-stable D-aminoacylase from microorganisms belonging to the genus Streptomyces by combining various purification methods. Furthermore, the present inventors found that the purified heat-stable D-aminoacylase is useful in industrial production of D-amino acids. By utilizing the heat-stable D-aminoacylase, it is possible to readily and efficiently produce the corresponding D-amino acids from N-acetyl-DL-amino acids (for example, N-acetyl-DL-methionine, N-acetyl-DL-valine, N-acetyl-DL-tryptophan, N-acetyl-DL-phenylalanine, N-acetyl-DL-alanine, N-acetyl-DL-leucine, and so on).

Abstract: A process is provided for delaying the deactivation of glutaryl amidase during catalysis. The amidase is, after maximum conversion of a substrate, separated off by filtration and can be reused in a subsequent reaction batch. In each reaction cycle, the amidase loses activity. The inactivation of the amidase can be delayed by bringing it into contact with a thiol during the reaction. The thiol is preferably 2-mercaptoethanol or cysteine.

Abstract: The present invention provides a cyclic lipopeptide acrylase which may effectively deacylate the acyl side chain of a cyclic lipopeptide compound, specifically FR901379 Substance or its analog thereof shown by the following general formula [I], and a process for production of a cyclic peptide compound which comprises the use of said acylase.