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Literature summary for 4.1.2.19 extracted from

  • Grueninger, D.; Schulz, G.E.
    Antenna domain mobility and enzymatic reaction of L-rhamnulose-1-phosphate aldolase (2008), Biochemistry, 47, 607-614.
    View publication on PubMed
Search for more literature for 4.1.2.19

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli strain JM105 Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant enzymes by hanging drop vapour diffusion method, with 100 mM sodium acetate pH 4.5, 50% (v/v) ethylene glycol and 5% (w/v) PEG1000 Escherichia coli

Protein Variants

Protein Variants Comment Organism
K15W reduced activity Escherichia coli
K15Y reduced activity Escherichia coli
K248G/R253A/E254A/E192A reduced activity Escherichia coli
L84W reduced activity Escherichia coli
Q11W reduced activity Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.9
-
 L-rhamnulose 1-phosphate mutant enzyme Q11W, in 60 mM Tris-HCl pH 7.5, 60 mM KCl Escherichia coli
2
-
 L-rhamnulose 1-phosphate mutant enzyme K15W, in 60 mM Tris-HCl pH 7.5, 60 mM KCl Escherichia coli
2
-
 L-rhamnulose 1-phosphate wild type enzyme, in 60 mM Tris-HCl pH 7.5, 60 mM KCl Escherichia coli
2.5
-
 L-rhamnulose 1-phosphate mutant enzyme K15Y, in 60 mM Tris-HCl pH 7.5, 60 mM KCl Escherichia coli
5.4
-
 L-rhamnulose 1-phosphate mutant enzyme L84W, in 60 mM Tris-HCl pH 7.5, 60 mM KCl Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P32169
-
-

Purification (Commentary)

Purification (Comment) Organism
Superdex 200 gel filtration Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Rhamnulose 1-phosphate
-
 Escherichia coli Glycerone phosphate + (S)-lactaldehyde
-
 ?

Synonyms

Synonyms Comment Organism
L-Rhamnulose-1-phosphate aldolase
-
 Escherichia coli
RhuA
-
 Escherichia coli