The three proline residues (P25, P242, and P434) of Agrobacterium CP4 5-enolpyruvylshikimate-3-phosphate synthase are crucial for the enzyme activity
- The three proline residues (P25, P242, and P434) of Agrobacterium CP4 5-enolpyruvylshikimate-3-phosphate synthase are crucial for the enzyme activity
- 강경수; 김영매; 전혜성; 박상령; 송대근; 이주영; 판철호; 김민균
- Agrobacterium sp. strain CP4; 5-Enolpyruvylshikimate-3-phosphate synthase; Glyphosate; Herbicide resistance; Proline residue
- Issue Date
- Plant biotechnology reports.
- VOL 4, NO 4, 329-334
- 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.
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