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Literature summary extracted from

  • Rice, E.A.; Bannon, G.A.; Glenn, K.C.; Jeong, S.S.; Sturman, E.J.; Rydel, T.J.
    Characterization and crystal structure of lysine insensitive Corynebacterium glutamicum dihydrodipicolinate synthase (cDHDPS) protein (2008), Arch. Biochem. Biophys., 480, 111-121.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.3.3.7 expressed in Escherichia coli STBL2, pET23b vector Corynebacterium glutamicum

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.3.3.7 hanging drop method, data collection and refinement statistics, refinement resolution originally extended to 3.0 A, gradually increased to 2.5 A, and finally to 2.2 A, structural similarities to other dihydrodipicolinate synthase Corynebacterium glutamicum

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.3.7 3-Bromopyruvate competitive inhibition, pyruvate as varied substrate Corynebacterium glutamicum
4.3.3.7 L-aspartate competitive inhibition, L-aspartate 4-semialdehyde as varied substrate Corynebacterium glutamicum
4.3.3.7 L-aspartate 4-semialdehyde uncompetitive inhibition by high concentrations of, no overcome by increasing pyruvate concentrations from 5 to 15 mM Corynebacterium glutamicum
4.3.3.7 L-lysine lack of feedback inhibition, not regulated under normal physiological conditions Corynebacterium glutamicum
4.3.3.7 oxaloacetate non-competitive inhibition, pyruvate as varied substrate Corynebacterium glutamicum
4.3.3.7 Succinic semialdehyde uncompetitive inhibition, L-aspartate 4-semialdehyde as varied substrate Corynebacterium glutamicum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.3.7 0.32
-
 pyruvate 2.5 mM pyruvate replaced by 0.1-2 mM, no substrate inhibition observed at high concentrations of pyruvate Corynebacterium glutamicum
4.3.3.7 0.63
-
 L-aspartate 4-semialdehyde reaction mixture includes 100 mM Tris-HCl, 2.5 mM pyruvate, 0.05-0.1 microg dihydrodipicolinate synthase and 0.2 mM NADPH, from 5.6 to 22.4 mM plots deviate from typical Michaelis-Menten kinetics, increased concentration fits an uncompetitive substrate inhibition model Corynebacterium glutamicum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.3.3.7 73000
-
 approximating the size of two DHDPS proteins interacting to form a dimer Corynebacterium glutamicum
4.3.3.7 158000
-
 native protein, gel filtration, homotetramer predicted Corynebacterium glutamicum

Organism

EC Number Organism UniProt Comment Textmining
4.3.3.7 Corynebacterium glutamicum P19808
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.3.7 gel filtration, SDS-PAGE Corynebacterium glutamicum

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.3.3.7 additional information
-
 structure in vicinity of the putative binding site for S-lysine indicates that the allosteric binding site in the Escherichia coli dihydrodipicolinate synthase does not exist in the enzyme of Corynebacterium glutamicum, difference of three non-conservative amino acids substitutions, explains lack of feedback inhibition by lysine in Corynebacterium glutamicum Corynebacterium glutamicum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.3.7 L-aspartate 4-semialdehyde + pyruvate lysine insensitivity of dihydrodipicolinate synthase analyzed, catalytic lysine residue forms a Schiff base adduct with pyruvate, active site lysine residues (K176a, K176b) Corynebacterium glutamicum dihydrodipicolinate + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
4.3.3.7 homotetramer ribbons rendition of homotetramer in the crystal lattice shown Corynebacterium glutamicum

Synonyms

EC Number Synonyms Comment Organism
4.3.3.7 cDHDPS
-
 Corynebacterium glutamicum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.3.3.7 213
-
 L-aspartate 4-semialdehyde
-
 Corynebacterium glutamicum

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
4.3.3.7 660
-
 5 mM pyruvate, addition of 0-716 mM lysine, lack of feedback inhibition Corynebacterium glutamicum L-lysine