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Literature summary for 4.1.2.52 extracted from

  • Wang, W.; Seah, S.Y.
    The role of a conserved histidine residue in a pyruvate-specific class II aldolase (2008), FEBS Lett., 582, 3385-3388.
    View publication on PubMed
Search for more literature for 4.1.2.52

Cloned(Commentary)

Cloned (Comment) Organism
mutant HpaI enzymes expressed in Escherichia coli Bl21(lambda DE3) cells Escherichia coli

Protein Variants

Protein Variants Comment Organism
H45A by site-directed mutagenesis, mutant enzyme has 24fold higher dissociation constant for Co2+ compared to the wild-type enzyme, apparent Km value for Co2+ increases by about 800fold compared to the wild-type enzyme, different kcat and km values Escherichia coli
H45Q by site-directed mutagenesis, mutant enzyme has 69fold higher dissociation constant for Co2+ compared to the wild-type enzyme, apparent Km value for Co2+ increases by about 800fold compared to the wild-type enzyme, different kcat and km values Escherichia coli

General Stability

General Stability Organism
the engineering results show that His45 has a structural and catalytic role. It is important for metal cofactor binding, possibly by proper positioning of a metal cofactor water ligand and is also involved in base catalysis. Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information apparent Km values for Co2+ increase in the two mutants H45A and H45Q by about 800fold compared to the wild-type enzyme Escherichia coli
0.38
-
 4-hydroxy-2-oxopentanoic acid wild-type, pH 8.0, 25°C Escherichia coli
16
-
 4-hydroxy-2-oxopentanoic acid H45Q mutant enzyme, pH 8.0, 25°C Escherichia coli
38
-
 4-hydroxy-2-oxopentanoic acid H45A mutant enzyme, pH 8.0, 25°C Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
additional information H45A and H45Q mutant enzymes have 24fold and 69fold higher dissociation constants for Co2+ compared to the wild-type enzyme Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 sizes of the native mutant enzymes are identical to that of the wild-type enzyme as determined by gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli Q47098
-
-

Purification (Commentary)

Purification (Comment) Organism
by anion exchange, hydrophobic interaction, and gel filtration chormatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-hydroxy-2-oxopentanoic acid
-
 Escherichia coli pyruvate + ?
-
 ?

Synonyms

Synonyms Comment Organism
HpaI
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.17
-
 4-hydroxy-2-oxopentanoic acid H45Q mutant enzyme, pH 8.0, 25°C Escherichia coli
4.5
-
 4-hydroxy-2-oxopentanoic acid H45A mutant enzyme, pH 8.0, 25°C Escherichia coli
350
-
 4-hydroxy-2-oxopentanoic acid wild-type, pH 8.0, 25°C Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
5 9
-
 Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.011
-
 4-hydroxy-2-oxopentanoic acid H45Q mutant enzyme, pH 8.0, 25°C Escherichia coli
0.12
-
 4-hydroxy-2-oxopentanoic acid H45A mutant enzyme, pH 8.0, 25°C Escherichia coli
930
-
 4-hydroxy-2-oxopentanoic acid wild-type, pH 8.0, 25°C Escherichia coli