Suntory Limited

Other

Hisayuki Matsuo

Kensaku Mizuno

Shoji Tanaka

Kazuhiro Ohsuye

Katsuhiko Kitano

Takaharu Tanaka

Takehiro Oshima

Masayasu Kojima

A C-terminal &agr;-amidating enzyme of and precursor thereof produced by a recombinant DNA technique; a DNA coding for the enzyme or precursor thereof; a plasmid containing the DNA; a host organism transformed with the plasmid; a process for production of the enzyme using the transformant; and a process for production of a C-terminal &agr;-amidated peptide using the enzyme.

Enzymatic production of a C-terminal &agr;-amidated peptide or protein

A C-terminal &agr;-amidating enzyme of,and precursor thereof produced by a recombinant DNA technique; a DNA coding for the enzyme or precursor thereof; a plasmid containing the DNA; a host organism transformed with the plasmid; a process for production of the enzyme using the transformant; and a process for production of a C-terminal &agr;-amidated peptide using the enzyme.

Recombinant C-terminal &agr;-amidating enzyme

A C-terminal .alpha.-amidating enzyme of Xenopus laevis and precursor thereof produced by a recombinant DNA technique; a DNA coding for the enzyme or precursor thereof; a plasmid containing the DNA; a host organism transformed with the plasmid; a process for production of the enzyme using the transformant; and a process for production of a C-terminal .alpha.-amidated peptide using the enzyme.

Recombinant C-terminal .alpha.-amidating enzyme

The invention relates to a C-terminal .alpha.-amidating enzyme of porcine origin having the following properties: (1) the action is on a peptide or protein represented by the formula:

C-terminal .alpha.-amidating enzyme and process for production thereof

A KEX2 endoprotease produced by a recombinant DNA technique, a KEX2 endoprotease shortened at the C-terminal of a native enzyme and still containing a C-terminal hydrophobic region, a soluble KEX2 endoprotease without a C-terminal hydrophobic region; DNA's coding for the above-mentioned enzymes; expression plasmids containing the DNA; hosts transformed with the plasmid; a process for production of the above-mentioned enzymes using the transformed host; and a process for production of biologically active polypeptide using the above-mentioned enzyme.

DNA encoding a KEX2 endoprotease without a C-terminal hydrophobic region

KEX2 endoprotease without a C-terminal hydrophobic region

C-terminal .alpha.-amidating enzyme preparations, including preparations AE-I, AE-II, AE-IIa and AE-IIb, from the skin of Xenopus laevis, wherein all components can convert a peptide having a glycine residue at its C-terminal to a C-terminal amidated peptide lacking the glycine residue, and have a common N-terminal amino acid sequence represented by Ser-Leu-Ser---, and AE-I and AE-IIa have a molecular weight of about 39,000, AE-IIb has a molecular weight of about 34,000, and AE-II comprises two components having molecular weight of about 39,000 and 34,000; a process for production of the above-mentioned enzyme preparations; and a process for .alpha.-amidation of a peptide by using the above mentioned enzyme preparations.

C-terminal alpha-amidating enzyme and process for production and use

Disclosed is a new protease having the following properties: (1) it is able to hydrolitically cleave a peptide bond between two adjacent basic amino acids in a peptide chain; (2) it has a molecular weight of about 43,000 as determined by electrophoresis; (3) it is inhibited by phenylmethylsulphonyl fluoride and diisopropyl fluorophosphate, but is not inhibited by monoiodoacetate, p-chloromercuribenzoic acid, ethylenediaminetetraacetic acid, 1,10-phenanthroline, tosyl-L-lysine chloromethyl ketone, and leupeptin. The protese can be produced by culturing Saccharomyces cerevisiae, and recovering purification by conventional methods, and is useful as a processing enzyme for conversion of a prohormone to an active hormone.

Protease and process for production and use thereof

Disclosed is a new protease having the following properties: (1) it is able to hydrolitically cleave a peptide bond between two adjacent basic amino acids in a peptide chain; (2) it has a molecular weight of about 43,000 as determined by electrophoresis; (3) it is inhibited by phenylmethylsulphonyl fluoride and diisopropyl fluorophosphate, but is not inhibited by monoiodoacetate, p-chloromercuribenzoic acid, ethylenediaminetetraacetic acid, 1,10-phenanthroline, tosyl-L-lysine chloromethyl ketone, and leupeptin. The protease can be produced by culturing Saccharomyces cerevisiae, and recovering purification by conventional methods, and is useful as a processing enzyme for conversion of a prohormone to an active hormone.

Growing community of inventors

Miyazaki, Japan

Kensaku Mizuno