TAILIEUCHUNG - Báo cáo khoa học: The product chain length determination mechanism of type II geranylgeranyl diphosphate synthase requires subunit interaction

The product chain length determination mechanism of type II geranyl-geranyl diphosphate synthase from the bacterium, Pantoea ananatis, was studied. In most types of short-chain (all-E) prenyl diphosphate synthases, bulky amino acids at the fourth and/or fifth positions upstream from the first aspartate-rich motif play a primary role in the product determination mechanism. | ỊFEBS Journal The product chain length determination mechanism of type II geranylgeranyl diphosphate synthase requires subunit interaction Motoyoshi Noike1 2 Takashi Katagiri1 Toru Nakayama1 Tanetoshi Koyama2 Tokuzo Nishino1 and Hisashi Hemmi1 1 Department of Biochemistry and Engineering Graduate Schoolof Engineering Tohoku University Miyagi Japan 2 Institute of Multidisciplinary Research for Advanced Materials Tohoku University Miyagi Japan Keywords farnesyldiphosphate synthase geranylgeranyl diphosphate synthase isoprenoid mutagenesis prenyltransferase Correspondence H. Hemmi Department of Applied Molecular Bioscience Graduate Schoolof BioagriculturalSciences Nagoya University Furo-cho Chikusa-ku Nagoya Aichi 464-8601 Japan Fax 81 52 789 4120 Tel 81 52 789 4134 E-mail hhemmi@ Received 21 February 2008 revised 2 June 2008 accepted 4 June 2008 doi The product chain length determination mechanism of type II geranylgeranyl diphosphate synthase from the bacterium Pantoea ananatis was studied. In most types of short-chain all-E prenyl diphosphate synthases bulky amino acids at the fourth and or fifth positions upstream from the first aspartate-rich motif play a primary role in the product determination mechanism. However type II geranylgeranyl diphosphate synthase lacks such bulky amino acids at these positions. The second position upstream from the G Q E motif has recently been shown to participate in the mechaism of chain length determination in type III geranylgeranyl diphosphate synthase. Amino acid substitutions adjacent to the residues upstream from the first aspartate-rich motif and from the G Q E motif did not affect the chain length of the final product. Two amino acid insertion in the first aspartate-rich motif which is typically found in bacterial enzymes is thought to be involved in the product determination mechanism. However deletion mutation of the insertion had no effect on product chain length. Thus .

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