BRENDA - Enzyme Database show

Evidence of allosteric enzyme regulation via changes in conformational dynamics A hydrogen/deuterium exchange investigation of dihydrodipicolinate synthase

Sowole, M.A.; Simpson, S.; Skovpen, Y.V.; Palmer, D.R.; Konermann, L.; Biochemistry 55, 5413-5422 (2016)

Data extracted from this reference:

Application
EC Number
Application
Commentary
Organism
4.3.3.7
drug development
the enzyme is a promising antibiotic target
Campylobacter jejuni
4.3.3.7
pharmacology
the enzyme is a promising antibiotic target
Campylobacter jejuni
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
4.3.3.7
bis-lysine
-
Campylobacter jejuni
4.3.3.7
L-lysine
allosteric inhihitor. Allostery is mediated by changes in the extent of thermally activated conformational fluctuations
Campylobacter jejuni
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.3.3.7
pyruvate + L-aspartate-4-semialdehyde
Campylobacter jejuni
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.3.3.7
Campylobacter jejuni
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.3.3.7
pyruvate + L-aspartate-4-semialdehyde
-
747107
Campylobacter jejuni
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
4.3.3.7
tetramer
-
Campylobacter jejuni
Application (protein specific)
EC Number
Application
Commentary
Organism
4.3.3.7
drug development
the enzyme is a promising antibiotic target
Campylobacter jejuni
4.3.3.7
pharmacology
the enzyme is a promising antibiotic target
Campylobacter jejuni
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
4.3.3.7
bis-lysine
-
Campylobacter jejuni
4.3.3.7
L-lysine
allosteric inhihitor. Allostery is mediated by changes in the extent of thermally activated conformational fluctuations
Campylobacter jejuni
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.3.3.7
pyruvate + L-aspartate-4-semialdehyde
Campylobacter jejuni
-
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
-
?
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.3.3.7
pyruvate + L-aspartate-4-semialdehyde
-
747107
Campylobacter jejuni
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
4.3.3.7
tetramer
-
Campylobacter jejuni
General Information
EC Number
General Information
Commentary
Organism
4.3.3.7
metabolism
the enzyme catalyzes a step of the diaminopimelate biosynthetic pathway of lysine
Campylobacter jejuni
General Information (protein specific)
EC Number
General Information
Commentary
Organism
4.3.3.7
metabolism
the enzyme catalyzes a step of the diaminopimelate biosynthetic pathway of lysine
Campylobacter jejuni