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Literature summary extracted from

  • Chou, C.Y.; Ko, T.P.; Wu, K.J.; Huang, K.F.; Lin, C.H.; Wong, C.H.; Wang, A.H.
    Modulation of substrate specificities of D-sialic acid aldolase through single mutations of Val-251 (2011), J. Biol. Chem., 286, 14057-14064.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.2.23 expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.2.23 in complex with hydroxypyruvate, hanging drop vapor diffusion method, using 2.0 M ammonium sulfate and 0.1 M Bis-Tris, pH 6.5 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.2.23 181
-
N-acetyl-D-mannosamine in 50 mM Tris-HCl, pH 7.8, at 37°C Escherichia coli
4.1.2.23 199
-
L-arabinose in 50 mM Tris-HCl, pH 7.8, at 37°C Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.2.23 sulfate one sulfate ion is found adjacent to the side chain of Lys-165 in the active site and another one on the surface of RS-aldolase Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.1.2.23 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.2.23 Ni-NTA column chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.2.23 3-deoxy-L-manno-octulosonate
-
Escherichia coli pyruvate + L-arabinose
-
r
4.1.2.23 D-sialic acid the RS-aldolase has a 5.8fold higher cleavage rate toward 3-deoxy-L-manno-octulosonate than toward D-sialic acid Escherichia coli N-acetyl-D-mannosamine + pyruvate
-
r
4.1.2.23 N-acetyl-D-mannosamine + pyruvate
-
Escherichia coli D-sialic acid
-
r
4.1.2.23 pyruvate + L-arabinose
-
Escherichia coli 3-deoxy-L-manno-octulosonate
-
r

Synonyms

EC Number Synonyms Comment Organism
4.1.2.23 D-sialic acid aldolase mutant V251I the mutant shows modified substrate specificity from D-sialic acid to 3-deoxy-L-manno-octulosonate Escherichia coli
4.1.2.23 L-3-deoxy-manno-2-octulosonic acid aldolase formerly Escherichia coli
4.1.2.23 L-KDO aldolase formerly Escherichia coli
4.1.2.23 RS-aldolase
-
Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.2.23 1.1
-
N-acetyl-D-mannosamine in 50 mM Tris-HCl, pH 7.8, at 37°C Escherichia coli
4.1.2.23 7.3
-
L-arabinose in 50 mM Tris-HCl, pH 7.8, at 37°C Escherichia coli

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.1.2.23 0.0055
-
N-acetyl-D-mannosamine in 50 mM Tris-HCl, pH 7.8, at 37°C Escherichia coli
4.1.2.23 0.04
-
L-arabinose in 50 mM Tris-HCl, pH 7.8, at 37°C Escherichia coli