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

BRENDA support

Literature summary for 4.1.2.17 extracted from

  • Joerger, A.C.; Mueller-Dieckmann, C.; Schulz, G.E.
    Structures of L-fuculose-1-phosphate aldolase mutants outlining motions during catalysis (2000), J. Mol. Biol., 303, 531-543.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method Escherichia coli

Protein Variants

Protein Variants Comment Organism
E73Q no enzyme activity Escherichia coli
E73Q/Y113F/Y209F no enzyme activity Escherichia coli
E73S no enzyme activity Escherichia coli
N29L decreased kcat, increased Km Escherichia coli
N29L/S71A no enzyme activity Escherichia coli
S71N no enzyme activity Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.2
-
L-Fuculose 1-phosphate pH 7.5, 37°C, wild-type Escherichia coli
130
-
L-Fuculose 1-phosphate pH 7.5, 37°C, N29Q mutant Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+
-
Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-fuculose 1-phosphate Escherichia coli
-
glycerone phosphate + (S)-lactaldehyde
-
r

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AB87
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-fuculose 1-phosphate
-
Escherichia coli glycerone phosphate + (S)-lactaldehyde
-
r

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.5
-
L-Fuculose 1-phosphate pH 7.5, 37°C, N29Q mutant Escherichia coli
19
-
L-Fuculose 1-phosphate pH 7.5, 37°C, wild-type Escherichia coli