Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.1.3.3 extracted from

  • Joerger, A.C.; Mayer, S.; Fersht, A.R.
    Mimicking natural evolution in vitro: an N-acetylneuraminate lyase mutant with an increased dihydrodipicolinate synthase activity (2003), Proc. Natl. Acad. Sci. USA, 100, 5694-5699.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.3.3

Crystallization (Commentary)

Crystallization (Comment) Organism
L142R mutant, complexed with beta-hydroxypyruvate, hanging drop vapor diffusion method Escherichia coli

Protein Variants

Protein Variants Comment Organism
L142R increased activity towards L-aspartate-beta-semialdehyde Escherichia coli
L142R/Y190D/E192A less efficient than wild-type enzyme Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
L-lysine 50% inhibition at 0.2 mM, inhibits wild-type enzyme, but not mutant enzymes Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6L4
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information One point mutation (L142R) is sufficient to create an enzyme that can complement a bacterial auxotroph lacking the gene for dihydrodipicolinate synthase, EC 4.2.1.52. The mutant enzyme catalyzes the reaction: L-aspartate 4-semialdehyde + pyruvate = dihydrodipicolinate + 2 H2O Escherichia coli ?
-
 ?
N-Acetylneuraminic acid
-
 Escherichia coli N-Acetyl-D-mannosamine + pyruvate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.8
-
 N-acetylneuraminic acid pH 7.2, 25°C, L142R/Y190D/E192A mutant Escherichia coli
7.7
-
 N-acetylneuraminic acid pH 7.2, 25°C, wild-type Escherichia coli
12.1
-
 N-acetylneuraminic acid pH 7.2, 25°C, L142R mutant Escherichia coli