···A novel gnd mutation leading to increased L-lysine production in Corynebacterium glutamicum.pdf

···A novel gnd mutation leading to increased L-lysine production in Corynebacterium glutamicum.pdf

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···A novel gnd mutation leading to increased L-lysine production in Corynebacterium glutamicum

FEMS Microbiology Letters 242 (2005) 265–274 A novel gnd mutation leading to increased LL-lysine production in Corynebacterium glutamicum Junko Ohnishi a, Ritsuko Katahira a, Satoshi Mitsuhashi a, Shingo Kakita a, Masato Ikeda b,* a Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., Asahi-machi, Machida, Tokyo 194-8533, Japan b Department of Bioscience and Biotechnology, Faculty of Agriculture, Shinshu University, Minami-minowa, Kami-ina, Nagano 399-4598, Japan Received 31 August 2004; received in revised form 2 November 2004; accepted 6 November 2004 First published online 19 November 2004 Edited by A. Yokota Abstract Toward more efficient LL-lysine production, we have been challenging genome-based strain breeding by the approach of assem- bling only relevant mutations in a single wild-type background. Following the creation of a new LL-lysine producer Corynebacterium glutamicum AHP-3 that carried three useful mutations (lysC311, hom59, and pyc458 ) on the relevant downstream pathways, we shifted our target to the pentose phosphate pathway. Comparative genomic analysis for the pathway between a classically derived LL-lysine producer and its parental wild-type identified several mutations. Among these mutations, a Ser-361 ! Phe mutation in the 6-phosphogluconate dehydrogenase gene (gnd) was defined as a useful mutation for LL-lysine production. Introduction of the gnd mutation into strain AHP-3 by allelic replacement led to approximately 15% increased LL-lysine production. Enzyma

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