The three proline residues (P25, P242, and P434) of Agrobacterium CP4 5-enolpyruvylshikimate-3-phosphate synthase are crucial for the enzyme activity

Title
The three proline residues (P25, P242, and P434) of Agrobacterium CP4 5-enolpyruvylshikimate-3-phosphate synthase are crucial for the enzyme activity
Authors
강경수김영매전혜성박상령송대근이주영판철호김민균
Keywords
Agrobacterium sp. strain CP4; 5-Enolpyruvylshikimate-3-phosphate synthase; Glyphosate; Herbicide resistance; Proline residue
Issue Date
2010-10
Publisher
Plant biotechnology reports.
Citation
VOL 4, NO 4, 329-334
Abstract
Multiple sequence alignments showed that the prolines at the 25th, 129th, 153rd, 242nd, 322nd, and 434th amino acids in 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) from Agrobacterium sp. strain CP4 are strongly conserved in various prokaryotic EPSPS proteins. Single point mutations of the conserved prolines to alanine (P25A, P153A, P242A, P322A, and P434A) were introduced in the CP4 EPSPS in order to investigate the importance of the conserved prolines for the enzyme properties. The point mutations caused decreases in substrate binding affinity and catalytic efficiency as well as the glyphosate resistance, in general. Especially, the 25th and 242nd prolines located in the polypeptide hinges connecting top and bottom domains of CP4 EPSPS as well as the 434th proline at the C-terminus of the enzyme turned out to be crucial for the enzyme activity.
URI
http://pubs.kist.re.kr/handle/201004/38044
ISSN
1863-5466
Appears in Collections:
KIST Publication > Article
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