Abstract: This invention relates to a novel polyphosphate: AMP phosphotransferase (PAP), a gene coding this PAP, and their use. The PAP has the following properties: (A) action: catalyzing of the following two reactions: NMP+PolyP(n)?NDP+PolyP(n-1) dNMP+POlyP(n)?dNDP+PolyP(n-1) (wherein NMP represents nucleoside monophosphate, NDP represents nucleoside diphosphate, dNMP represents deoxynucleoside monophosphate, dNDP represents deoxynucleoside diphosphate, n represents degree of polymerization of the polyphosphate which is an integer of up to 100); (B) substrate specificity: specific to AMP, GMP, IMP, dAMP, and dGMP, also acting with CMP, UMP, dCMP, and TMP; (C) molecular weight: about 55 to 56 Kd (kilodalton); and (D) specific activity: at least 70 units per 1 mg of enzyme protein.

Abstract: The present invention describes synthetic peptide substrates of the metalloproteases, aggrecanase-1 and/or -2 suitable for assays of enzyme activity. The invention also describes methods using these peptides to discover pharmaceutical agents that modulate these proteases.

Abstract: DNA isolates coding for human DNase and methods of obtaining such DNA are provided, together with expression systems for recombinant production of human DNase useful in therapeutic or diagnostic compositions.

Abstract: The present invention provides a method for producing L-glutamic acid by fermentation, by culturing in a liquid medium a microorganism that can metabolize a carbon source at a specific pH, and wherein said medium contains a carbon source and L-glutamic acid at a saturation concentration, and wherein said microorganism is able to cause accumulation of an amount of L-glutamic acid in a liquid medium having said pH, wherein said amount exceeds the amount of L-glutamic acid at said saturation concentration when the pH of the medium is controlled so that L-glutamic acid is precipitated, making L-lysine exist in the medium when L-glutaminc acid concentration is lower than the concentration at which natural crystallization of L-glutamic acid occurs, and precipitating the ?-form crystals of L-glutamic acid.

Abstract: DNA and recombinant DNA that encode a peptide-forming enzyme, a method for producing a peptide-forming enzyme, and a method for producing a dipeptide are disclosed. A method for producing a dipeptide includes producing a dipeptide from a carboxy component and an amine component by using a culture of a microbe belonging to the genus Sphingobacterium and having the ability to form the dipeptide from the carboxy component and the amine component, a microbial cell separated from the culture, treated microbial cell product of the microbe or a peptide-forming enzyme derived from the microbe.

Abstract: The present invention provides a method for producing dipeptide using inexpensively acquirable starting materials by an industrially advantageous and simple pathway. Dipeptide is produced from L-amino acid ester and L-amino acid using a culture of microbes having the ability to produce a dipeptide from an L-amino acid ester and an L-amino acid, using microbial cells isolated from the culture, or a treated microbial cell product of the microbe.

Abstract: The present invention provides mutant D-aminoacylases and use thereof. The mutant D-aminoacylases are hard to be inhibited by the substrate and, comprise the amino acid sequences of the D-aminoacylase derived from Alcaligenes denitrificans subsp. xylosoxydans MI-4 strain, wherein amino acid residues at specific sites have been modified. The mutants of the present invention have high reaction specificity as well as resistance to inhibition by the substrate. The present invention enables high-yield production of D-amino acids using higher concentrations of N-acyl-DL-amino acid as the substrate. The mutants of the present invention are useful in producing D-tryptophan in particular.

Abstract: Disclosed are various forms of an active, isolated ?-secretase enzyme in purified and recombinant form. This enzyme is implicated in the production of amyloid plaque components which accumulate in the brains of individuals afflicted with Alzheimer's disease. Recombinant cells that produce this enzyme either alone or in combination with some of its natural substrates (?-APPwt and ?-APPsw) are also disclosed, as are antibodies directed to such proteins. These compositions are useful for use in methods of selecting compounds that modulate ?-secretase. Inhibitors of ?-secretase are implicated as therapeutics in the treatment of neurodegenerative diseases, such as Alzheimer's disease.

Abstract: Disclosed are various forms of an active, isolated ?-secretase enzyme in purified and recombinant form. This enzyme is implicated in the production of amyloid plaque components which accumulate in the brains of individuals afflicted with Alzheimer's disease. Recombinant cells that produce this enzyme either alone or in combination with some of its natural substrates (?-APPwt and ?-APPsw) are also disclosed, as are antibodies directed to such proteins. These compositions are useful for use in methods of selecting compounds that modulate ?-secretase. Inhibitors of ?-secretase are implicated as therapeutics in the treatment of neurodegenerative diseases, such as Alzheimer's disease.

Abstract: The present invention provides a human polypeptide homolog of DBF4/ASK1 (for “Activator of S phase kinase”) and polynucleotides which identify and encode DRF1 (for “DBF4 Related Factor 1”). In addition, the invention provides expression vectors, host cells and methods for its production. The invention also provides methods for the identification of DRF1 or DRF1-containing complex agonists/antagonists, useful for the treatment of human diseases and conditions.

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

Abstract: Disclosed are various forms of an active, isolated ?-secretase enzyme in purified and recombinant form. This enzyme is implicated in the production of amyloid plaque components which accumulate in the brains of individuals afflicted with Alzheimer's disease. Recombinant cells that produce this enzyme either alone or in combination with some of its natural substrates (?-APPwt and ?-APPsw) are also disclosed, as are antibodies directed to such proteins. These compositions are useful for use in methods of selecting compounds that modulate ?-secretase. Inhibitors of ?-secretase are implicated as therapeutics in the treatment of neurodegenerative diseases, such as Alzheimer's disease.

Abstract: Isolated ASMT nucleic acid molecules that include a nucleotide sequence variant and nucleotides flanking the sequence variant are described, as well as ASMT allozymes. Methods for determining if a mammal is at risk for toxicity from acute or chronic arsenic exposure also are described.

Abstract: Fusion proteins of protease inhibitors are provided, in particular fusion proteins of alpha 1-antitrypsin (AAT) and a second protease inhibitor, such as secretory leukocyte protease inhibitor (SLPI) or tissue inhibitor of metalloproteases (TIMP). Polynucleotides encoding the fusion proteins, vectors comprising such polynucleotides, and host cells containing such vectors are also provided. Methods of making the fusion proteins of the invention are also provide, as well as methods of using the fusion proteins, for example to inhibit protease activity in a biological sample or in the treatment of an individual suffering from, or at risk for, a disease or disorder involving unwanted protease activity.

Abstract: The present invention relates to isolated nucleic acid molecules encoding mutants of glucose-6-phosphate dehydrogenase, and vectors and hosts cells including such nucleic acid molecules. These nucleic acid molecules are involved in the biosynthesis of a fine chemical, e.g., an amino acid such as lysine. The present invention also relates to methods of producing and modulating the production of fine chemicals, e.g., lysine, by culturing recombinant microorganisms containing these nucleic acid molecules under conditions such that the fine chemical is produced.

Abstract: A method for efficient production of an S-hydroxynitrile lyase by gene recombination using Escherichia coli is provided. A gene is formed by altering a codon in an S-hydroxyniitrylase gene originating in cassava (Manihot esculenta Crantz) without changing the amino acid sequence thereof till the frequency of codon usage wholly with an amino acid in Escherichia coli reaches a level of not less than 5%. According to the method for the production of an S-hydroxynitrile lyase by the use of the gene, the S-hydroxynitrile lyase can be produced in a large amount with an unusually high yield.

Abstract: The invention provides compositions and methods related to human telomerase reverse transcriptase (hTRT), the catalytic protein subunit of human telomerase. The polynucleotides and polypeptides of the invention are useful for diagnosis, prognosis and treatment of human diseases, for changing the proliferative capacity of cells and organisms, and for identification and screening of compounds and treatments useful for treatment of diseases such as cancers.

Abstract: The subject of the present invention is to provide a ?-lactam acylase protein having high activity, a gene coding for said ?-lactam acylase protein, a recombinant vector having said gene, a transformant containing said recombinant vector, and a method of producing a ?-lactam antibiotic such as amoxycillin using said ?-lactam acylase. A ?-lactam acylase gene of Stenotrophomonas maltophilia was cloned, the DNA base sequence and the amino acid sequence expected therefrom was determined, and a Stenotrophomonas ?-lactam acylase gene was obtained. This gene was found to code for a protein with a molecular weight of about 70 kDa and having ?-lactam acylase activity, and could efficiently produce amoxycillin without being inhibited by phenylacetic acid, etc. Furthermore, by modification of the amino acid sequence, a protein which can more efficiently produce amoxycillin could be obtained.

Abstract: (1) A modified sarcosine oxidase with improved stability in the acidic range compared to a wild-type sarcosine oxidase. (2) A sarcosine oxidase gene encoding a modified sarcosine oxidase of the following (a), (b), or (c): (a) protein composed of the amino acid sequence represented by SEQ ID NO: 1 (b) protein composed of an amino acid sequence wherein one or some amino acid(s) are deleted, substituted, or added from the amino acid sequence represented by SEQ ID NO: 1, and which has sarcosine oxidase activity (c) protein composed of an amino acid sequence which shows 80% or more homology to the amino acid sequence represented by SEQ ID NO: 1, and which has sarcosine oxidase activity According to the present invention, sarcosine oxidases, in particular sarcosine oxidases which show optimal pH and high activity in the slightly acidic range and have improved stability can be prepared efficiently, thus making the invention industrially useful.

Abstract: This invention relates to newly identified polypeptides which have zinc metalloprotease activities and are referred to as IGS5, and polynucleotides encoding such polypeptides, to their use in therapy and in identifying compounds which may be stimulators and/or inhibitors which are useful in therapy, and to production of such polypeptides and polynucleotides.