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Literature summary for 4.1.2.4 extracted from

  • Ma, H.; Szeler, K.; Kamerlin, S.C.L.; Widersten, M.
    Linking coupled motions and entropic effects to the catalytic activity of 2-deoxyribose-5-phosphate aldolase (DERA) (2016), Chem. Sci., 7, 1415-1421 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.2.4

Application

Application Comment Organism
synthesis the enzyme is an interesting candidate for bio-catalysis of carbo-ligation reactions, which are central to synthetic chemistry Escherichia coli

Protein Variants

Protein Variants Comment Organism
S238P completely abolished catalytic activity in the retro-aldol reaction Escherichia coli
S238P/S239P completely abolished catalytic activity in the retro-aldol reaction Escherichia coli
S239P the mutant enzyme increases the enthalpy change at the transition state, relative to the wild-type enzyme, but concomitant loss in entropy causes an overall relative loss in the TS free energy change. This entropy loss, as measured by the temperature dependence of catalysed rates, is mirrored in both a drastic loss in dynamics of the enzyme, which contributes to phosphate binding, as well as an overall loss in anti-correlated motions distributed over the entire protein Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.096
-
 2-deoxy-D-ribose 5-phosphate pH 8.0, 30°C, wild-type enzyme Escherichia coli
3
-
 2-deoxy-D-ribose 5-phosphate pH 8.0, 30°C, mutant enzyme S239P Escherichia coli
9.6
-
 2-deoxy-D-ribose 5-phosphate pH 8.0, 30°C, mutant enzyme S238I/S239I Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6L0
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-deoxy-D-ribose 5-phosphate
-
 Escherichia coli D-glyceraldehyde 3-phosphate + acetaldehyde
-
 r
D-glyceraldehyde 3-phosphate + acetaldehyde
-
 Escherichia coli 2-deoxy-D-ribose 5-phosphate
-
 r

Synonyms

Synonyms Comment Organism
2-Deoxyribose-5-phosphate aldolase
-
 Escherichia coli
DERA
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4
-
 2-deoxy-D-ribose 5-phosphate pH 8.0, 30°C, mutant enzyme S238I/S239I Escherichia coli
11
-
 2-deoxy-D-ribose 5-phosphate pH 8.0, 30°C, mutant enzyme S239P Escherichia coli
15
-
 2-deoxy-D-ribose 5-phosphate pH 8.0, 30°C, wild-type enzyme Escherichia coli

General Information

General Information Comment Organism
metabolism the enzyme is involved in the pentose phosphate pathway Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.15
-
 2-deoxy-D-ribose 5-phosphate pH 8.0, 30°C, mutant enzyme S238I/S239I Escherichia coli
3.6
-
 2-deoxy-D-ribose 5-phosphate pH 8.0, 30°C, mutant enzyme S239P Escherichia coli
130
-
 2-deoxy-D-ribose 5-phosphate pH 8.0, 30°C, wild-type enzyme Escherichia coli