Abstract: A process for industrially advantageously producing a dipeptide via a convenient pathway starting with less expensive and easily available materials is provided. A dipeptide is produced from an L-amino acid amide and an L-amino acid by using a culture of a microbe capable of synthesizing the dipeptide from the L-amino acid amide and the L-amino acid, microbial cells separated from the culture or a treated microbial cell product from the microbe. An L-amino acid amide hydrolase is obtained from a microbe belonging to the genus erwinia, genus Rhodococcus, genus Chryseobacterium, genus Micrococcus, genus Cryptococcus, genus Trichosporion, genus Rhodosporidium, genus Sporobolomyces, genus Tremela, genus Torulaspora, genus Sterigmatomyces or genus Rhodotorula. The hydrolase catalyzes a reaction that produces a dipeptide from an L-amino acid amide and an L-amino acid.

Abstract: A method for producing ?-hydroxy amino acid and its optically-active isomer is provided. The ?-hydroxy amino acid is produced by reacting a predetermined D-?-amino acid and 5,10-methylene tetrahydrofolic acid in the presence of an enzyme derived from a microorganism belonging to the genera Paracoccus, Aminobacter, or Ensifer.

Abstract: The present invention relates to a 5-substituted hydantoin racemase, which efficiently catalyzes racemization reactions at a high optimum temperature for racemization reactions, DNA coding for the racemase, and processes for producing optically active amino acids.

Abstract: The present invention provides a method of producing optically active amino acids from 5-substituted hydantoin by isolating a hydantoinase gene and an N-carbamyl-L-amino acid hydrolase gene involved in an ability to convert 5-substituted hydantoin or N-carbamylamino acid into optically active amino acids from a microorganism of the genus Microbacterium having the above ability and by improving gene amplification and transcriptional and translational activities thereby preparing a recombinant wherein the amount of the desired enzymes produced is increased. The hydantoinase gene is, for example, a DNA encoding for a protein having a hydantoinase activity, which has the nucleotide sequence set forth in SEQ ID NO:1 in the Sequence. The N-carbamyl-L-amino acid hydrolase gene is, for example, a DNA encoding for a protein having an N-carbamyl-L-amino acid hydrolase activity, which has the nucleotide sequence set forth in SEQ ID NO:3 in the Sequence.

Abstract: A method for producing a dipeptide including the step of exposing a carboxy component and an amine component to an enzyme having an activity to hydrolyze amino acid ester. Such a hydrolase has been found among enzymes in bacteria. The method is useful for producing a peptide simply and inexpensively with a high yield without taking complicate synthetic methods.

Abstract: The present invention relates to a 5-substituted hydantoin racemase, which efficiently catalyzes racemization reactions at a high optimum temperature for racemization reactions, DNA coding for the racemase, and processes for producing optically active amino acids.

Abstract: DNA for encoding a protein having D-hydantoinase activity which has a base sequence represented by Sequence ID No. 1 in the Sequence Listing. DNA for encoding a protein having D-carbamylase activity which has a base sequence represented by Sequence ID No. 3 in the Sequence Listing.

Abstract: The present invention provides a method of producing optically active amino acids from 5-substituted hydantoin by isolating a hydantoinase gene and an N-carbamyl-L-amino acid hydrolase gene involved in an ability to convert 5-substituted hydantoin or N-carbamylamino acid into optically active amino acids from a microorganism of the genus Microbacterium having the above ability and by improving gene amplification and transcriptional and translational activities thereby preparing a recombinant wherein the amount of the desired enzymes produced is increased. The hydantoinase gene is, for example, a DNA encoding for a protein having a hydantoinase activity, which has the nucleotide sequence set forth in SEQ ID NO:1 in the Sequence. The N-carbamyl-L-amino acid hydrolase gene is, for example, a DNA encoding for a protein having an N-carbamyl-L-amino acid hydrolase activity, which has the nucleotide sequence set forth in SEQ ID NO:3 in the Sequence.

Abstract: DNA for encoding a protein having D-hydantoinase activity which has a base sequence represented by Sequence ID No. 1 in the Sequence Listing. DNA for encoding a protein having D-carbamylase activity which has a base sequence represented by Sequence ID No. 3 in the Sequence Listing.

Abstract: The present invention is to provide an excellent peptide-synthesizing protein and a method for efficiently producing a peptide. A peptide is synthesized by reacting an amine component and a carboxy component in the presence of at least one of proteins shown in the following (I) and (II): (I) The mutant protein having the amino acid sequence containing one or more mutations of the above mutations 1 to 38 in the amino acid sequence described in SEQ ID NO:2; and (II) The mutant protein having the amino acid sequence containing one or more mutations selected from the group consisting of substitution, deletion, insertion, addition and inversion at positions other than one or more mutation positions of the above mutation 1 to 38 in the mutant protein described in the above (I), and having a peptide-synthesizing activity.

Abstract: DNA for encoding a protein having D-hydantoinase activity which has a base sequence represented by Sequence ID No. 1 in the Sequence Listing. DNA for encoding a protein having D-carbamylase activity which has a base sequence represented by Sequence ID No. 3 in the Sequence Listing.

Abstract: A novel protein which has an activity to transport hydantoin compounds is described, as well as a recombinant expressing this transporter protein. From Microbacterium liquefaciens strain AJ3912, a novel gene was discovered to encode a protein which is able to transport hydantoin compounds. A recombinant with an excellent ability to uptake hydantoin compounds is obtained by introducing and expressing the novel gene, called mhp, using gene recombination techniques.

Abstract: The present invention provides a method for producing a dipeptide from starting materials that are available at low costs through a route industrially advantageous and simple. Dipeptides are produced from amino acid esters and amino acids by using a culture of a microbe having an ability to produce a dipeptide from an amino acid ester and an amino acid, microbial cells separated from the culture, or treated microbial cell product.

Abstract: DNA for encoding a protein having D-hydantoinase activity which has a base sequence represented by Sequence ID No. 1 in the Sequence Listing. DNA for encoding a protein having D-carbamylase activity which has a base sequence represented by Sequence ID No. 3 in the Sequence Listing.

Abstract: A process for industrially advantageously producing a dipeptide via a convenient pathway starting with less expensive and easily available materials is provided. A dipeptide is produced from an L-amino acid amide and an L-amino acid by using a culture of a microbe capable of synthesizing the dipeptide from the L-amino acid amide and the L-amino acid, microbial cells separated from the culture or a treated microbial cell product from the microbe. An L-amino acid amide hydrolase is obtained from a microbe belonging to the genus erwinia, genus Rhodococcus, genus Chryseobacterium, genus Micrococcus, genus Cryptococcus, genus Trichosporion, genus Rhodosporidium, genus Sporobolomyces, genus Tremela, genus Torulaspora, genus Sterigmatomyces or genus Rhodotorula. The hydrolase catalyzes a reaction that produces a dipeptide from an L-amino acid amide and an L-amino acid.

Abstract: The present invention provides a method for industrially producing an optically active lysine derivative useful as a pharmaceutical intermediate. More particularly, the present invention provides a production method including protecting an amino group or an amino group and carboxyl group of optically active 2-amino-6-methyl-6-nitroheptanoic acid with a protecting group, reducing a nitro group to synthesize a 6,6-dimethyl lysine derivative and reacting the 6,6-dimethyl lysine derivative with an acetic acid derivative.

Abstract: The present invention provides a method for industrially producing an optically active lysine derivative useful as a pharmaceutical intermediate. More particularly, the present invention provides a production method including protecting an amino group or an amino group and carboxyl group of optically active 2-amino-6-methyl-6-nitroheptanoic acid with a protecting group, reducing a nitro group to synthesize a 6,6-dimethyl lysine derivative and reacting the 6,6-dimethyl lysine derivative with an acetic acid derivative.

Abstract: A 2?-deoxyribonucleoside is produced by culturing a microorganism, which is transformed with a gene encoding a ribonucleotide reductase and in which 2?-deoxyribonucleoside degradation activity is decreased or eliminated by disrupting a gene encoding a purine nucleoside phosphorylase on chromosomal DNA, in a medium in which the microorganism can grow to produce the 2?-deoxyribonucleoside.

Abstract: A method for producing a dipeptide including the step of exposing a carboxy component and an amine component to an enzyme having an activity to hydrolyze amino acid ester. Such a hydrolase has been found among enzymes in bacteria. The method is useful for producing a peptide simply and inexpensively with a high yield without taking complicate synthetic methods.

Abstract: The present invention provides a method for producing the peptides comprising: cultivating in medium the microorganisms wherein at least one gene selected from the group consisting of a gene encoding; aminoacylhistidine peptidase; a gene encoding leucylaminopeptidase; and a gene encoding isoaspartyldipeptidase, respectively; has been disrupted on the chromosome and wherein preferably transformed with the recombinant DNA, comprising polynucleotide encoding the proteins having peptide-synthesizing activity, mixing at least one of the cultivated microorganisms and the disrupted cells of the microorganisms with the carboxy and amine components for the peptide synthesis.