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Literature summary for 4.1.2.55 extracted from

  • Royer, S.F.; Haslett, L.; Crennell, S.J.; Hough, D.W.; Danson, M.J.; Bull, S.D.
    Structurally informed site-directed mutagenesis of a stereochemically promiscuous aldolase to afford stereochemically complementary biocatalysts (2010), J. Am. Chem. Soc., 132, 11753-11758.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Saccharolobus solfataricus

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray crystallographic analysis of the active site of the aldolase bound to pyruvate, 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate at 4°C, reveals that its catalytic mechanism is typical of the N-acetylneuraminic acid lyase superfamily Saccharolobus solfataricus

Protein Variants

Protein Variants Comment Organism
T157C improved for 2-dehydro-3-deoxy-D-gluconate with a 75% diastereoisomeric ratio Saccharolobus solfataricus
T157C/Y132V diastereoselective formation of 2-dehydro-3-deoxy-D-gluconate with much improved (91%) diastereoisomeric ratio Saccharolobus solfataricus
T157F/Y132V diastereoselective formation of 2-dehydro-3-deoxy-D-gluconate with much improved (93%) diastereoisomeric ratio Saccharolobus solfataricus
T157V/A198L/D181Q diastereoselective formation of 2-dehydro-3-deoxy-D-galactonate with much improved (88%) diastereoisomeric ratio Saccharolobus solfataricus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1
-
pyruvate 70°C, pH is not specified in the publication, wild-type enzyme Saccharolobus solfataricus
4.1
-
pyruvate 70°C, pH is not specified in the publication, mutant enzyme T157F/Y132V Saccharolobus solfataricus
5.3
-
D-glyceraldehyde 70°C, pH is not specified in the publication, wild-type enzyme T157F/Y132V Saccharolobus solfataricus
8
-
D-glyceraldehyde 70°C, pH is not specified in the publication, mutant enzyme Saccharolobus solfataricus
9.1
-
D-glyceraldehyde 70°C, pH is not specified in the publication, mutant enzyme T157C/Y132V Saccharolobus solfataricus
39.6
-
pyruvate 70°C, pH is not specified in the publication, mutant enzyme T157C/Y132V Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus O54288
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + D-glyceraldehyde the enzyme exhibits poor diastereocontrol in many of its aldol reactions, including the reaction of its natural substrates, pyruvate and D-glyceraldehyde, which afford a 55:45 mixture of D-2-keto-3-deoxygluconate and D-2-keto-3-deoxy-galactonate Saccharolobus solfataricus 2-dehydro-3-deoxy-D-galactonate
-
r
pyruvate + D-glyceraldehyde the enzyme exhibits poor diastereocontrol in many of its aldol reactions, including the reaction of its natural substrates, pyruvate and D-glyceraldehyde, which afford a 55:45 mixture of D-2-keto-3-deoxygluconate and D-2-keto-3-deoxy-galactonate Saccharolobus solfataricus 2-dehydro-3-deoxy-D-gluconate
-
r

Synonyms

Synonyms Comment Organism
2-keto-3-deoxygluconate aldolase
-
Saccharolobus solfataricus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.06
-
D-glyceraldehyde 70°C, pH is not specified in the publication, mutant enzyme Saccharolobus solfataricus
0.07
-
pyruvate 70°C, pH is not specified in the publication, mutant enzyme T157C/Y132V Saccharolobus solfataricus
0.07
-
D-glyceraldehyde 70°C, pH is not specified in the publication, mutant enzyme T157C/Y132V Saccharolobus solfataricus
0.075
-
pyruvate 70°C, pH is not specified in the publication, mutant enzyme T157F/Y132V Saccharolobus solfataricus
4.6
-
pyruvate 70°C, pH is not specified in the publication, wild-type enzyme Saccharolobus solfataricus
5.5
-
D-glyceraldehyde 70°C, pH is not specified in the publication, wild-type enzyme T157F/Y132V Saccharolobus solfataricus