Toyota Jidosha Kabushiki Kaisha

Japan Science and Technology Corporation

International Flower Developments Proprietary Limited

Tokuzo Nishino

Chikara Ohto

Shinichi Ohnuma

Kazutake Hirooka

Shusei Obata

Tanetoshi Koyama

Chika Asada

Yoshihiro Sato

Yoshie Takeuchi

Keishi Narita

Hisashi Hemmi

Hiroyuki Nakane

Toru Nakayama

Chika Ishida

Keiko Sakakibara

Kyozo Ogura

Ayumi Koike

Yuka Higuchi

Shin-ichi Ohnuma

Manabu Suzuki

Takeshi Nakazawa

Naoki Tsuruoka

Minoru Akai

A mutant prenyl diphosphate synthase capable of synthesizing prenyl diphosphates, shorter than those synthesized by the original enzyme, by modifying the amino acid sequence in and upstream of the aspartic acid-rich domain DDXX (XX)D (X denotes any amino acid, and XX in the parentheses may not be present) present in region II of the prenyl diphosphate synthase.

Mutant prenyl diphosphate synthase

A protein which has an amino acid sequence shown by SEQ ID NO: 2, 4, 6, 23, 25, 27 or 29, or any of these amino acid sequences modified, and which has activity for transferring an aliphatic acyl group to a glycosyl group at the 5-position of flavonoids, and a gene encoding the same.

Aliphatic acyl transferase genes

Bacillus sp. NTAP-1 having been deposited under accession number FERM BP-6926; and a collagen-decomposing enzyme produced by bacterium. The above enzyme (1) has a capability of hydrolyzing, at the highest efficiency, collagen and gelatin from among casein, gelatin, albumin and collagen; (2) shows the optimum pH of 3.5 to 4.5; (3) shows the optimum temperature of 65 to 70&deg; C.; (4) after heating at 60&deg; C. at pH 6.0 for 4 hours, sustains an activity amounting to 60% or more of the level before the heat treatment; (5) remains stable at pH 3 to 6; and a molecular weight of approximately 46,000 when measured by SDS-PAGE.

Thermostable collagen-digesting enzyme, novel microorganism producing the enzyme and process for producing the enzyme

The present invention provides a prenyl diphosphate synthetase and a gene coding for the synthetase. The invention discloses a recombinant protein having the amino acid sequence shown in SEQ ID NO:2 or a recombinant protein which has the amino acid sequence shown in SEQ ID NO:2 having deletion, substitution or addition of at least one amino acid and which has decaprenyl diphosphate synthetase activity; a gene coding for the protein; a recombinant vector comprising the gene; a transformant transformed with the vector; a method for producing a decaprenyl diphosphate synthetase; and a method for producing ubiquinone-10.

Decaprenyl diphosphate synthetase gene

An isolated recombinant protein comprising the amino acid sequence shown in SEQ ID No: 1 is disclosed. A preferred embodiment of the invention is a recombinant protein having the amino acid sequence shown in SEQ ID NO: 1 but having a deletion, substitution or addition of at least one amino acid, excluding the amino acid at position 82, and which has geranyl diphosphate synthase activity. Also disclosed is the gene encoding the recombinant protein.

Geranyl diphosphate synthase genes

A mutant prenyl diphosphate synthase having a modified amino acid sequence of prenyl diphosphate synthase, wherein the amino acid residue located at the eighth position in the N-terminal direction from D of the N-terminal of the Asp-rich domain DDXX(XX)D (in the sequence X denotes any amino acid and the two X's in the parentheses may not be present) present in the region II has been substituted by another amino acid, or both of the amino acid residue located at the fifth position in the N-terminal direction from D of the N-terminal and the amino acid residue located at the eighth position in the N-terminal direction from D of the N-terminal have been substituted by other amino acids.

Mutated prenyl diphosphate synthases

Manufacture or use of a mutant prenyl diphosphate synthase in which the amino acid residue located at the fifth position in the N-terminal direction from D of the N-terminal of the aspartic acid-rich domain DDXX(XX)D (the two X's in the parentheses may not be present) present in the second region among the conserved regions of the prenyl diphosphate synthase has been substituted by another amino acid.

Mutant prenyl diphosphate synthase, DNA encoding mutant prenyl diphosphate synthase and process for producing mutant prenyl phosphate synthase

A mutant prenyl diphosphate synthase capable of synthesizing prenyl diphosphates, shorter than those synthesized by the original enzyme, by modifying the amino acid sequence in and upstream of the aspartic acid-rich domain DDXX(XX)D (X denotes any amino acid, and XX in the parentheses may not be present) present in region II of the prenyl diphosphate synthase.

Farnesyl diphosphate synthase

The present invention discloses a mutated enzyme comprising a geranylgeranil diphosphate synthase having its origin in wild type Sulfolobus acidocaldarius wherein at least one of phenylalanine at position 77, methionine at position 85, valine at position 99, tyrosine at position 101, phenylalanine at position 118, arginine at position 199 and aspartic acid at position 312 is substituted with another amino acid.

Process for the production of prenyl diphosphate using mutants of

The present invention discloses a mutated enzyme comprising a geranylgeranil diphosphate synthase having its origin in wild type Sulfolobus acidocaldarius wherein, at least one of phenylalanine at position 77, methionine at position 85, valine at position 99, tyrosine at position 101, phenylalanine at position 118, arginine at position 199 and aspartic acid at position 312 is substituted with another amino acid.

Nucleic acid encoding mutant geranylgeranyl diphosphate synthase

Long-chain prenyl diphosphate synthase

DNA coding for thermostable geranylgeranyl diphosphate (GGDP) synthase derived from Sulfolobus acidocaldarius is provided. The DNA is useful for production of GGDP synthase, which is, in turn, useful for production of GGDP.

Growing community of inventors

Sendai, Japan

Tokuzo Nishino