Characterization and crystal structure of lysine insensitive Corynebacterium glutamicum dihydrodipicolinate synthase (cDHDPS) protein

The lysine insensitive Corynebacterium glutamicum dihydrodipicolinate synthase enzyme (cDHDPS) was recently successfully introduced into maize plants to enhance the level of lysine in the grain. To better understand lysine insensitivity of the cDHDPS, we expressed , purified, kinetically characteriz...

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Bibliographic Details
Published in:Archives of biochemistry and biophysics 2008-12, Vol.480 (2), p.111-121
Main Authors: Rice, Elena A., Bannon, Gary A., Glenn, Kevin C., Jeong, Soon Seog, Sturman, Eric J., Rydel, Timothy J.
Format: Article
Language:English
Subjects:
ADDUCTS
Amino Acid Sequence
AMINO ACIDS
Catalytic Domain
Characterization
Corynebacterium glutamicum
Corynebacterium glutamicum - enzymology
CRYSTAL STRUCTURE
Crystallography, X-Ray - methods
DHDPS enzyme
Electrophoresis, Polyacrylamide Gel
ENZYMES
ESCHERICHIA COLI
Escherichia coli - enzymology
FEEDBACK
Humans
Hydro-Lyases - chemistry
Inhibitory Concentration 50
Insensitivity to lysine
Kinetic properties
Kinetics
LEVELS
LYSINE
Lysine - chemistry
MAIZE
MATERIALS SCIENCE
Models, Biological
Molecular Sequence Data
PLANTS
Protein Structure, Tertiary
PROTEINS
RESIDUES
SCHIFF BASES
Sequence Homology, Amino Acid
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Summary:The lysine insensitive Corynebacterium glutamicum dihydrodipicolinate synthase enzyme (cDHDPS) was recently successfully introduced into maize plants to enhance the level of lysine in the grain. To better understand lysine insensitivity of the cDHDPS, we expressed , purified, kinetically characterized the protein, and solved its X-ray crystal structure. The cDHDPS enzyme has a fold and overall structure that is highly similar to other DHDPS proteins. A noteworthy feature of the active site is the evidence that the catalytic lysine residue forms a Schiff base adduct with pyruvate. Analyses of the cDHDPS structure in the vicinity of the putative binding site for S-lysine revealed that the allosteric binding site in the Escherichia coli DHDPS protein does not exist in cDHDPS due to three non-conservative amino acids substitutions, and this is likely why cDHDPS is not feedback inhibited by lysine.
ISSN:0003-9861
1096-0384
DOI:10.1016/j.abb.2008.09.018