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

BRENDA support

Literature summary for 4.1.2.19 extracted from

  • Garrabou, X.; Joglar, J.; Parella, T.; Crehuet, R.; Bujons, J.; Clapés, P.
    Redesign of the phosphate binding site of L-rhamnulose-1-phosphate aldolase towards a dihydroxyacetone dependent aldolase (2011), Adv. Synth. Catal., 353, 89-99.
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli strain M-15 Escherichia coli

Protein Variants

Protein Variants Comment Organism
N29D the mutant shows 5.3% of the wild type activity, the mutation increases by 3fold the Vappmax of aldol addition reactions of dihydroxyacetone to other aldehyde acceptors rather than the natural L-lactaldehyde Escherichia coli
N32D the mutant shows 0.1% of the wild type activity Escherichia coli
S116D the mutant shows 0.2% of the wild type activity Escherichia coli
S75D the mutant shows 0.1% of the wild type activity Escherichia coli
T115D completely inactive Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
phosphate the aldol addition of dihydroxyacetobe is strongly inhibited by phosphate Escherichia coli
sulfate
-
Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.6
-
dihydroxyacetone phosphate wild type enzyme, apparent value, at pH 7.0 and 25°C Escherichia coli
7
-
dihydroxyacetone phosphate mutant enzyme N29D, apparent value, at pH 7.0 and 25°C Escherichia coli
1125
-
dihydroxyacetone wild type enzyme, apparent value, at pH 7.0 and 25°C Escherichia coli
1339
-
dihydroxyacetone mutant enzyme N29D, apparent value, at pH 7.0 and 25°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P32169
-
-

Purification (Commentary)

Purification (Comment) Organism
HR 16/40 afinity column chromatography Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.002
-
mutant enzyme S75D, using L-rhamnulose-1-phosphate as substrate, at pH 7.0 and 25°C Escherichia coli
0.005
-
mutant enzyme N32D, using L-rhamnulose-1-phosphate as substrate, at pH 7.0 and 25°C Escherichia coli
0.006
-
mutant enzyme S116D, using L-rhamnulose-1-phosphate as substrate, at pH 7.0 and 25°C Escherichia coli
0.2
-
mutant enzyme N29D, using L-rhamnulose-1-phosphate as substrate, at pH 7.0 and 25°C Escherichia coli
3.8
-
wild type enzyme, using L-rhamnulose-1-phosphate as substrate, at pH 7.0 and 25°C Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(benzyloxy)acetaldehyde + dihydroxyacetone favored direction of reaction Escherichia coli (3R,4S)-5-(benzyloxy)-1,3,4-trihydroxypentan-2-one + (3R,4R)-5-(benzyloxy)-1,3,4-trihydroxypentan-2-one
-
r
benzyl (2-oxoethyl)carbamate + dihydroxyacetone favored direction of reaction Escherichia coli benzyl [(2S,3R)-2,3,5-trihydroxy-4-oxopentyl]carbamate + benzyl [(2R,3R)-2,3,5-trihydroxy-4-oxopentyl]carbamate
-
r
benzyl [(2R)-1-oxopropan-2-yl]carbamate + dihydroxyacetone favored direction of reaction Escherichia coli benzyl [(2R,3S,4R)-3,4,6-trihydroxy-5-oxohexan-2-yl]carbamate + benzyl [(2R,3R,4R)-3,4,6-trihydroxy-5-oxohexan-2-yl]carbamate
-
r
dihydroxyacetone + L-lactaldehyde favored direction of reaction Escherichia coli L-rhamnulose 1-phosphate
-
r
dihydroxyacetone phosphate + L-lactaldehyde
-
Escherichia coli ?
-
?
dihydroxyacetone phosphate + L-lactaldehyde favored direction of reaction Escherichia coli L-rhamnulose 1-phosphate
-
r
L-rhamnulose 1-phosphate
-
Escherichia coli dihydroxyacetone phosphate + L-lactaldehyde
-
r
N-formylglycinal + dihydroxyacetone
-
Escherichia coli N-[(2S,3R)-2,3,5-trihydroxy-4-oxopentyl]formamide + N-[(2R,3R)-2,3,5-trihydroxy-4-oxopentyl]formamide
-
r

Synonyms

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

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.5
-
wild type enzyme, at pH 7.0 and 25°C Escherichia coli phosphate