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微生物酵素の生化学的及び構造生物学的研究と医療への応用


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Title: 微生物酵素の生化学的及び構造生物学的研究と医療への応用
Other Titles: Biochemistry and Structural Biology of Microbial Enzymes and their Medical Applications
Authors: 芳本, 忠
Authors (alternative): Yoshimoto, Tadashi
Issue Date: Jul-2007
Publisher: 日本薬学会 / The Pharmaceutical Society of Japan
Citation: YAKUGAKU ZASSHI v.127(7) p.1035-1045, 2007
Abstract: Microbial enzymes were studied from two medicinal viewpoints. First, we examined proline-specific peptidases from pathogenic microorganisms. We found several proline-specific peptidases in pathogenic bacteria. Among them, prolyl tripeptidyl aminopeptidase from Porphylomonas gingivals and prolyl aminopeptidase from Serratia marcescens were crystallized. The complex structures of those enzymes and inhibitors were clarified in X-ray crystallography. Aminopeptidase N, which has wide specificity for amino acids, was distributed in the pathogens. The crystal structure of the aminopeptidase N elucidated the reasons for its wide substrate specificity but inertness to the X-Pro bond. It was also revealed that proline-specific peptidases and aminopeptidase N cooperatively degrade collagen for the uptake of amino acids as nutrition when these bacteria infect cells. Second, we applied enzymes from microorganisms to diagnostic analyses. We found a series of creatinine-metabolizing enzymes in Pseudomonas putida. Creatininase, creatinase, and sarcosine oxidase were coupled and have been developed for a diagnostic analysis kit that examines renal function. The structures of the native and the Mn2+-activated creatininases were determined in X-ray crystallography. Based on the structure, the activated enzyme was used for an improved assay kit. The structure of D-3-hydroxybutyrate dehydrogenase from Pseudomonas fragi was also clarified in crystallography. The enzyme is useful for diagnostic analysis of diabetes mellitus while monitoring ketone bodies.
Keywords: structural biology / proline-specific peptidase / microbial enzyme / diagnostic analysis
URI: http://hdl.handle.net/10069/14912
ISSN: 00316903
DOI: 10.1248/yakushi.127.1035
Relational Links: http://dx.doi.org/10.1248/yakushi.127.1035
Type: Journal Article
Text Version: publisher
Appears in Collections:Articles in academic journal

Citable URI : http://hdl.handle.net/10069/14912

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