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Search for Microbial Enzymes Useful for Creatinine Assay

Research Project

Project/Area Number 01890007
Research Category

Grant-in-Aid for Developmental Scientific Research (B).

Allocation TypeSingle-year Grants
Research Field 広領域
Research InstitutionKyoto University

Principal Investigator

YAMADA Hideaki  Kyoto Univ. Agric. Professor, 農学部, 教授 (30027180)

Co-Investigator(Kenkyū-buntansha) NAGASAWA Toru  Kyoto Univ. Agric. Assist. Prof., 農学部, 助手 (60115904)
SHIMIZU Sakayu  Kyoto Univ. Agric. Assoc. Prof., 農学部, 助教授 (70093250)
IZUMI Yoshikazu  Tottori Univ. Engineering Professor, 工学部, 教授 (40026555)
Project Period (FY) 1989 – 1990
Project Status Completed (Fiscal Year 1990)
Budget Amount *help
¥8,100,000 (Direct Cost: ¥8,100,000)
Fiscal Year 1990: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 1989: ¥6,700,000 (Direct Cost: ¥6,700,000)
KeywordsCreatinine analysis / Enzymatic analysis / Creatinine deiminase / N-Methylhydantoin amidohydrolase / N-Carbamoylsarcosine amidohydrolase / Peroxidase / Sarcosine oxidase / N-メチルヒダントインアミドヒトロラ-ゼ / N-カルバモイルサルコシンアミドヒドロラ-ゼ
Research Abstract

A novel metabolic pathway for the degradation of creatinine with N-methylhydantoin, N-carbamoylsarcosine and sarcosine as successive intermediates was found to operate in Pseudomonas putida 77 and many other microorganisms. Enzymes involved in this pathway were purified from cells of P. Putida and characterized. The first step, deimination of creatinine, is catalyzed by cytosine deaminase/creatinine deiminase. The following two steps, ring-openinig of N-methylhydantoin and decarbamoylation of N-carbamoylsarcosine, are catalyzed by new enzymes, N-methylgydantoin amidohydrolase and N-carbamoylsarcosine amidohydrolase, respectively. The former enzyme requires ATP, Mg^<2+>, and for the hydrolysis and the reaction proceeds as follows : N-methylhydantoin ---> N-carbamoylsarcosine + ADP + Pi. The latter catalyzes the following reaction ; N-carbamoylsarcosine + H_20 ---> sarcosine + NH. Sarcosine dehydrogenase was found to be the responsible enzyme for the oxidation of sarcosine to glycine in P. Putida 77, but sarcosine oxidase was also found to be involved in this oxidation in several microorganisms. These enzymes were found to be useful for determination of creatinine.

Report

(3 results)
  • 1990 Annual Research Report   Final Research Report Summary
  • 1989 Annual Research Report
  • Research Products

    (7 results)

All Other

All Publications (7 results)

  • [Publications] Sakayu Shimizu: "Microbial enzymes for creatinine assay:a review" Clin.Chim.Acta. 185. 241-262 (1989)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1990 Final Research Report Summary
  • [Publications] Kengo Akimoto: "Luminol chemiluminescence reaction catalyzed by a microbial peroxidase" Anal.Biochem.189. 182-185 (1990)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1990 Final Research Report Summary
  • [Publications] Shimizu et al.: "Microbial enzymes for creatinine assay : a review" Clin. Chim. Acta. 185. 241-252 (1989)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1990 Final Research Report Summary
  • [Publications] K. Akimoto et al.: "Luminol chemiluminescence reaction catalyzed by a microbial peroxidase" Anal. Biochem.189. 182-185 (1990)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1990 Final Research Report Summary
  • [Publications] Sakayu Shimizu: "Microbial enzymes for creatinine assay:a review" Clin.Chim.Acta. 185. 241-262 (1989)

    • Related Report
      1990 Annual Research Report
  • [Publications] Kengo Akimoto: "Luminol chemiluminescence reaction catalyzed by a microbial peroxidase" Anal.Biochem.189. 182-185 (1990)

    • Related Report
      1990 Annual Research Report
  • [Publications] Sakayu Shimizu: "Microbial enzymes for creatinine assay:a review" Clin.Chim.Acta. 185. 241-252 (1989)

    • Related Report
      1989 Annual Research Report

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Published: 1989-04-01   Modified: 2016-04-21  

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