Structure, Function and Application of Quaternary Ammonium

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Structure Function and Application Structure Function and Application

TENTATIVE SCHEDULE 8/10/2009 (Thursday)

Structure, Function and Application of Quaternary Ammonium

Compound Degrading Enzymes

Prof Dr Mori Nobuhiro

Structure, Function and Application of Quaternary Ammonium

Prof Dr Mori Nobuhiro

8.30 am – 9:00 am Registration

9:15 am – 9:30 am Welcome Speech 9:30 am 10:40 am

Prof. Dr. Mori Nobuhiro

(Agriculture, Biological and Environmental Sciences, Tottori University, Japan. )

And

Aminopeptidases as Biocatalyst:

Prof. Dr. Mori Nobuhiro

(Agriculture, Biological and Environmental Sciences, Tottori University, Japan. )

And

Aminopeptidases as Biocatalyst:

9:30 am – 10:40 am

Seminar I: Structure, function and application of quaternary Ammonium Compound Degrading Enzymes

Prof.Dr. Mori Nobuhiro

10:40 am – 11:00 am Tea Break

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Practical Applications and Functional Modifications

Dr Arima Jiro

(Agriculture, Biological and Environmental

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Practical Applications and Functional Modifications

Dr Arima Jiro

(Agriculture, Biological and Environmental

11.00 am – 12.10 pm

Seminar II: Aminopeptidases as biocatalyst : Practical Application and Functional Modifications

Dr. Arima Jiro

12.10– 2.00 pm

Conclusion, Q&A and Wrap-up

8

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October Thursday 9:00 am ~ 12:30 pm

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Sciences, Tottori University, Japan.)

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Sciences, Tottori University, Japan.)

Conclusion, Q&A and Wrap up Lunch

Institute of Systems Biology INBIOSIS

Universiti Kebangsaan Malaysia

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PROF. DR. MORI NOBUHIRO Structure, Function and Application of Quaternary Ammonium

Senior Professor

School of Agriculture, Biological and Environmental Sciences Tottori University Japan

Sciences, Tottori University, Japan

Experiences:

Doctor of Philosophy PhD , Agriculture, Agricultural Chemistry, 1982, University of Kyoto Japan.

The microbial degradation and metabolism of quaternary ammonium compounds such as choline, L‐, and D‐carnitine have been investigated. L‐Carnitine dehydrogenases EC 1.1.1.108 were purified from Xanthomonas translucens and Rhizobium Pseudomonas sp. There were two differences,

Expert in microbial cells by using protein purification, characterization, enzyme kinetic, genomic approaches and analytical biochemistry

Published more than 50 papers in high impact journals

d i f th t i t f J S i t f

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molecular mass and Km value for L‐carnitine, between these enzymes. Structure and function of these enzymes are discussed.

D‐Carnitine dehydrogenase EC 1.1.1.254 fromAgrobacteriumsp.

was purified and characterized. Furthermore, enzymatic conversion of D‐carnintine to L‐carninitine was carried by intact cell reaction. Trimethylaminobutyraldehyde dehydrogenase and is one of the secretariats of Japan Society for

Bioscience, Biotechnology and Agrochemistry. One of the committee members for international proceeding, 2008 Annual Meeting: The Japan Society for

Bioscience, Biotechnology and Agrochemistry.

cell reaction. Trimethylaminobutyraldehyde dehydrogenase TMAB‐aldehyde DH, EC 1.2.1.47 from Pseudomonas sp. was purified and characterized. TMAB‐aldehyde DH I gene and II gene were found in the cell. Structure and function of these enzymes are discussed by homology modeling of betaine aldehyde dehydrogenase.

Appointed as the project leader of Development and Application of microbial enzyme and structure and function of quaternary ammonium compound degrading enzymes

Research Areas:

Microbial Biotechnology

Microbiology

Enzymology

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DR. ARIMA JIRO Aminopeptidases as biocatalyst : Practical applications and functional

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ly.

Practical applications and functional modifications

Junior Associate Professor

School of Agriculture, Biological and Environmental Sciences, Tottori University, Japan

Experiences:

Doctor of Philosophy PhD , Agriculture, Enzymology, Molecular Biology and

Bioengineering, 2003, University of Okayama Japan.

Involved in Functional analysis and molecular

Aminopeptidases APs remove the N‐terminal amino acid from proteins, small oligopeptides, or aminoacyl derivatives. There are some types in APs; for example, aminopepitdases belonging M family accommodate metal ions in their active sites, S and C

Involved in Functional analysis and molecular evolution of peptide hydrolases from

streptomyces, and enzymes for the synthesis of chiral amino acids and peptides, and molecular design of useful enzymes for industrial

applications.

family enzymes have respectively catalytic Ser or Cys residues in their active sites. The catalytic mechanisms of them are different from each other. Because the activities of APs are associated with many biological functions and play an important role in many pathological conditions, the catalytic mechanism and structure of APs are well known. Although the enzymes have

Publishedmore than 20 research journals in Protein Science, Enzyme and Microbial Technology,Biochimie, Applied Microbial and Biotechnology, Journal of Biochemical Chemistry and Biochimica et Biophysica Acta‐Proteins and

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many interesting and useful features, until recently, practical applications of bacterial APs had not been considered. This presentation focuses on practical applications and functional modification of bacterial APs belonging M and S family.

Proteomics.

His greatest findings has been patented and commercialized in Japan Aminopeptides for production of food additives, Nagase Co.Ltd, Japan .

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Research Areas:

Protein Engineering

Applied Biochemistry

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Registration Form

INBIOSIS Seminar Series 10 INBIOSIS Seminar Series 10

Name :

Institution :

Address :

Tel No. :

Fax No. :

Attendance confirmation should be made before 6

^th

OCTOBER 2009 Tuesday and sent to:

f l

Fax No. :

Email :

Institute of Systems Biology Universiti Kebangsaan Malaysia

43600 UKM Bangi or faxed to 03‐8921 3398

*As places are limited early registration is recommended As places are limited, early registration is recommended.

Enquires

For more information please contact:

03 8921 4561 / 4558 /4549

Cik Faridda Hannim / Pn.Rafidah Ahmad/ General / / Or email:

[email protected]/ [email protected]

/[email protected] Or Fax:

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