Partial Characterization of Dihydrobenzophenanthridine Oxidase and Its Role with Elicitation
Jeong Jin Park, Division of Molecular and life science, POSTECH, San31, Hyojadong, Pohang, 790-784, South Korea, Hwa-Young Cho, POSTECH, POSTECH, San 31, Pohang, 790784, South Korea, Sung-Yong H. Yoon, POSTECH, Env.Eng.Bldg. #416, Pohang, Kyungbuk 790-784, Korea, Seok-Young Son, POSTECH, POSTECH, Pohang, Kyungbuk 790-784, Korea, Hong Soon Rhee, Division of Molecular and life science, POSTECH, POSTECH, Pohang, Kyungbuk 790-784, Korea and Jong Moon Park, Division of Molecular and life science, POSTECH, POSTECH, Pohang, 790-784, South Korea

Sanguinarine is one of most effective material of antimicrobial and antifungal ingredients. In cell culture system of Eschscholtzia californica, healthy cell does not make sanguinarine but dihydrosanguinarine. It means that dihydrobenzophenanthridine oxidase (DHBO), which oxidase dihydroform benzophenanthridine alkaloids to their end product, is not expressed in normal cell culture condition. There are two ways to up-regulate DHBO expression level, one is using transformant cell and the other is elicitation. Up to now, only N-terminal sequence of DHBO was revealed. So we detected DHBO's protein spot location in 2D gel and got a N-terminal and C-terminal sequence. Many important changes in cellular metabolism and physiology of E. californica were identified by combined analysis of metabolome and proteome with elicitation. Using this method, we got the expression pattern of DHBO and other enzymes, which is related to dihydrosanguinarine production. In this research, we archive partial amino acid sequence of DHBO and expression pattern with elicitation.

Extended Abstract Status: Not Uploaded

Advances in Biocatalysis and Protein Engineering I

The Preliminary Program for 2005 Annual Meeting (Cincinnati, OH)