result 222 件
| FullText URL | K0007269_abstract_review.pdf |
|---|---|
| Author | REN, JIANCHAO| |
| Published Date | 2025-03-25 |
| Content Type | Thesis or Dissertation |
| Grant Number | 甲第7269号 |
| Granted Date | 2025-03-25 |
| Thesis Type | Doctor of Philosophy in Science |
| Grantor | 岡山大学 |
| language | English |
| FullText URL | K0007258_abstract_review.pdf K0007258_fulltext.pdf K0007258_other.pdf K0007258_summary.pdf |
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| Author | SEKI, Aiko| |
| Published Date | 2025-03-25 |
| Content Type | Thesis or Dissertation |
| Grant Number | 甲第7258号 |
| Granted Date | 2025-03-25 |
| Thesis Type | Doctor of Philosophy in Dental Science |
| Grantor | 岡山大学 |
| language | Japanese |
| FullText URL | K0007169_abstract_review.pdf K0007169_fulltext.pdf |
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| Author | CHAOMULIGE| |
| Published Date | 2024-09-25 |
| Content Type | Thesis or Dissertation |
| Grant Number | 甲第7169号 |
| Granted Date | 2024-09-25 |
| Thesis Type | Doctor of Philosophy |
| Grantor | 岡山大学 |
| language | Japanese |
| FullText URL | K0007039_abstract_review.pdf K0007039_fulltext.pdf |
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| Author | IIJIMA, Yuta| |
| Published Date | 2024-03-25 |
| Content Type | Thesis or Dissertation |
| Grant Number | 甲第7039号 |
| Granted Date | 2024-03-25 |
| Thesis Type | Doctor of Philosophy in Pharmaceutical Sciences |
| Grantor | 岡山大学 |
| language | Japanese |
| FullText URL | K0007030_abstract_review.pdf K0007030_fulltext.pdf K0007030_other.pdf K0007030_summary.pdf |
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| Author | ADACHI, Reimi| |
| Published Date | 2024-03-25 |
| Content Type | Thesis or Dissertation |
| Grant Number | 甲第7030号 |
| Granted Date | 2024-03-25 |
| Thesis Type | Doctor of Philosophy in Dental Science |
| Grantor | 岡山大学 |
| language | Japanese |
| FullText URL | K0007011_abstract_review.pdf K0007011_fulltext.pdf K0007011_other.pdf K0007011_summary.pdf |
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| Author | SANO, Sho| |
| Published Date | 2024-03-25 |
| Content Type | Thesis or Dissertation |
| Grant Number | 甲第7011号 |
| Granted Date | 2024-03-25 |
| Thesis Type | Doctor of Philosophy in Dental Science |
| Grantor | 岡山大学 |
| language | Japanese |
| FullText URL | O004054.pdf |
|---|---|
| Author | Tanioka, Hiroaki| |
| Published Date | 2005-09-30 |
| Content Type | Thesis or Dissertation |
| Grant Number | 乙第4054号 |
| Granted Date | 2005-09-30 |
| Thesis Type | Doctor of Philosophy in Medical Science |
| Grantor | 岡山大学 |
| language | English |
| FullText URL | K003043.pdf |
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| Author | 単 錦宇| |
| Published Date | 2005-09-30 |
| Content Type | Thesis or Dissertation |
| Grant Number | 甲第3043号 |
| Granted Date | 2005-09-30 |
| Thesis Type | Doctor of Philosophy in Engineering |
| Grantor | 岡山大学 |
| language | Japanese |
| FullText URL | K0006813_abstract_review.pdf K0006813_fulltext.pdf K0006813_other.pdf K0006813_summary.pdf |
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| Author | NAGATA, Chiaki| |
| Published Date | 2023-03-24 |
| Content Type | Thesis or Dissertation |
| Grant Number | 甲第6813号 |
| Granted Date | 2023-03-24 |
| Thesis Type | Doctor of Philosophy in Dental Science |
| Grantor | 岡山大学 |
| language | Japanese |
| Title Alternative | Studies on l-Glutamate Oxidase with Strict Substrate Specificity from Streptomyces sp. |
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| FullText URL | srfa_112_013_018.pdf |
| Author | Nakayama, Natsume| Inagaki, K.| |
| Abstract | l-glutamate oxidase (LGOX) from Streptomyces sp. is a heterohexameric flavin enzyme that catalyzes the oxidative deamination of l-glutamate to form α-ketoglutarate with ammonia and hydrogen peroxide. LGOX shows strict substrate specificity for l-Glu. In addition, it is highly thermostable and pH stable. Because of these properties, LGOX is currently used as a biosensor for the trace determination of l-Glu in the food industry and clinical laboratories. The full-length cDNA is 2103 bp and is encoded by a single polypeptide chain consisting of 701 residues including subunits α-γ-β. The LGOX gene was heterologously expressed in Escherichia coli JM109. The LGOX precursor expressed in E. coli is a homodimer with weak enzymatic activity and becomes a heterohexamer upon activation by protease treatment. X-ray crystallography and docking studies of purified recombinant LGOX suggest that the Arg305 residue is a key residue for substrate recognition. Mutant analysis showed that Arg305 is essential for substrate recognition, as the activity toward l-Glu was greatly reduced and substrate specificity was changed in some enzymes. The functional analysis of R305E-LGOX, which is an l-Arg oxidase, revealed that R305E-LGOX can be used as a enzyme biosensor for l-Arg. |
| Keywords | l-glutamate oxidase biosensor substrate recognition X-ray crystallography modification of substrate specificity |
| Publication Title | Scientific Reports of the Faculty of Agriculture, Okayama University |
| Published Date | 2023-02-01 |
| Volume | volume112 |
| Start Page | 13 |
| End Page | 18 |
| ISSN | 2186-7755 |
| language | Japanese |
| File Version | publisher |
| FullText URL | srfa_112_contents.pdf |
|---|---|
| Publication Title | Scientific Reports of the Faculty of Agriculture, Okayama University |
| Published Date | 2023-02-01 |
| Volume | volume112 |
| ISSN | 2186-7755 |
| language | Japanese |
| File Version | publisher |
| FullText URL | K0006706_abstract_review.pdf K0006706_fulltext.pdf K0006706_other.pdf K0006706_summary.pdf |
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| Author | YONEDA, Mitsuhiro| |
| Published Date | 2022-09-22 |
| Content Type | Thesis or Dissertation |
| Grant Number | 甲第6706号 |
| Granted Date | 2022-09-22 |
| Thesis Type | Doctor of Philosophy in Dental Science |
| Grantor | 岡山大学 |
| language | Japanese |
| FullText URL | K0006663_abstract_review.pdf K0006663_fulltext.pdf |
|---|---|
| Author | Monzur, Sadia| |
| Published Date | 2022-03-25 |
| Content Type | Thesis or Dissertation |
| Grant Number | 甲第6663号 |
| Granted Date | 2022-03-25 |
| Thesis Type | Doctor of Philosophy |
| Grantor | 岡山大学 |
| language | English |
| FullText URL | K0006660_abstract_review.pdf K0006660_fulltext.pdf K0006660_summary.pdf |
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| Author | Furuta, Takahiro| |
| Published Date | 2022-03-25 |
| Content Type | Thesis or Dissertation |
| Grant Number | 甲第6660号 |
| Granted Date | 2022-03-25 |
| Thesis Type | Doctor of Philosophy in Agriculture |
| Grantor | 岡山大学 |
| language | Japanese |
| FullText URL | K0006653_abstract_review.pdf K0006653_fulltext.pdf |
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| Author | Mimata, Yoshiharu| |
| Published Date | 2022-03-25 |
| Content Type | Thesis or Dissertation |
| Grant Number | 甲第6653号 |
| Granted Date | 2022-03-25 |
| Thesis Type | Doctor of Philosophy in Agriculture |
| Grantor | 岡山大学 |
| language | English |
| FullText URL | K0006652_abstract_review.pdf K0006652_fulltext.pdf |
|---|---|
| Author | Myojin, Takumi| |
| Published Date | 2022-03-25 |
| Content Type | Thesis or Dissertation |
| Grant Number | 甲第6652号 |
| Granted Date | 2022-03-25 |
| Thesis Type | Doctor of Philosophy in Agriculture |
| Grantor | 岡山大学 |
| language | Japanese |
| FullText URL | K0006651_abstract_review.pdf K0006651_fulltext.pdf |
|---|---|
| Author | Okawa, Atsushi| |
| Published Date | 2022-03-25 |
| Content Type | Thesis or Dissertation |
| Grant Number | 甲第6651号 |
| Granted Date | 2022-03-25 |
| Thesis Type | Doctor of Philosophy in Agriculture |
| Grantor | 岡山大学 |
| language | Japanese |
| FullText URL | srfa_111_contents.pdf |
|---|---|
| Publication Title | Scientific Reports of the Faculty of Agriculture, Okayama University |
| Published Date | 2022-02-01 |
| Volume | volume111 |
| ISSN | 2186-7755 |
| language | Japanese |
| File Version | publisher |
| Title Alternative | The List of Published by Members of the Faculty From January to December 2021 |
|---|---|
| FullText URL | srfa_111_027_042.pdf |
| Publication Title | Scientific Reports of the Faculty of Agriculture, Okayama University |
| Published Date | 2022-02-01 |
| Volume | volume111 |
| Start Page | 27 |
| End Page | 42 |
| ISSN | 2186-7755 |
| language | Japanese |
| File Version | publisher |
| Title Alternative | Studies on antitumor enzyme l-lysine α-oxidase from Trichoderma viride |
|---|---|
| FullText URL | srfa_111_007_014.pdf |
| Author | Saito, Masaya| Inagaki, Kenji| |
| Abstract | L-Lysine α-oxidase (LysOX) from Trichoderma viride is a homodimeric flavoenzyme that catalyzes the oxidative deamination of L-Lysine to produce α-keto-ε-aminocaproate with ammonia and hydrogen per-oxide. LysOX inhibited the growth of cancer cells but showed relatively low toxicity for normal cells. The full-length cDNA consists of 2,119 bp, and encodes a long N-terminal propeptide composed of 77 resi-dues (Met1-Arg77) and the mature protein (Ala78-Ile617). The LysOX gene was heterologously expressed in Streptomyces lividans TK24 or Escherichia coli SoluBL21. The enzymatic properties of the purified recombinant LysOX, such as substrate specificity, kinetic parameters and thermal stability, are the same as those of the native LysOX. The LysOX precursor (prLysOX) expressed in E. coli shows weak enzymatic activity and is activated by proteolytic processing. The crystal structure of prLysOX revealed that the propeptide of prLysOX indirectly changes the active site structure to inhibit enzyme activity. Moreover, the crystal structures of LysOX and its L-Lysine complex revealed that the hydrogen bonding network formed by Asp212, Asp315 and Ala440 with two water molecules is responsible for the recogni-tion of the ε-amino group of L-Lysine. In addition, a narrow substrate-binding site and acidic surface at the active site entrance both contribute to strict substrate specificity. Mutational analysis demonstrated that Asp212 and Asp315 are essential for substrate recognition, and the D212A/D315A LysOX prefers aromatic amino acids. Furthermore, the structural basis of the substrate specificity change has also been revealed by the structural analysis of the D212A/D315A LysOX and its substrate complexes. |
| Keywords | L-lysine α-oxidase antitumor enzyme substrate recognition X-ray crystallography enzyme activity regulation |
| Publication Title | Scientific Reports of the Faculty of Agriculture, Okayama University |
| Published Date | 2022-02-01 |
| Volume | volume111 |
| Start Page | 7 |
| End Page | 14 |
| ISSN | 2186-7755 |
| language | Japanese |
| File Version | publisher |
| NAID | 120007190707 |
