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Literature summary for 1.1.1.37 extracted from

  • Bjork, A.; Dalhus, B.; Mantzilas, D.; Sirevag, R.; Eijsink, V.G.
    Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface (2004), J. Mol. Biol., 341, 1215-1226.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapour-diffusion method Chloroflexus aurantiacus

Protein Variants

Protein Variants Comment Organism
E165K increase in temperature-optimum to 65°C, compared to 60°C for the wild-type enzyme. Maximal specific activity at temperature optimum is increased by about 30% compared to wild-type enzyme. Melting temperature at pH 4.4 is by 4.6°C, melting temperature at pH 6.0 is increased by 12.0°C and melting temperature at pH 7.5 is increased by 23.9°C compared to wild-type enzyme, mutation stabilizes to such an extent that disruption of the inter-dimer electrostatic network around residue 165 no longer limits kinetic thermal stability Chloroflexus aurantiacus
E165Q increase in temperature-optimum to 65°C, compared to 60°C for the wild-type enzyme. Maximal specific activity at temperature optimum is increased by about 30% compared to wild-type enzyme. Melting temperature at pH 4.4 is by 5.4°C, melting temperature at pH 6.0 is increased by 11.2°C and melting temperature at pH 7.5 is increased by 23.6°C compared to wild-type enzyme, mutation stabilizes to such an extent that disruption of the inter-dimer electrostatic network around residue 165 no longer limits kinetic thermal stability Chloroflexus aurantiacus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
32000
-
4 * 32000, SDS-PAGE Chloroflexus aurantiacus

Organism

Organism UniProt Comment Textmining
Chloroflexus aurantiacus P80040
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Chloroflexus aurantiacus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oxaloacetate + NADH
-
Chloroflexus aurantiacus L-malate + NAD+
-
?

Subunits

Subunits Comment Organism
tetramer 4 * 32000, SDS-PAGE Chloroflexus aurantiacus

Synonyms

Synonyms Comment Organism
CaMDH
-
Chloroflexus aurantiacus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
wild-type enzyme Chloroflexus aurantiacus
65
-
mutant enzyme E165Q and E165K Chloroflexus aurantiacus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
55 65 55°C: about 70% of maximal activity, 65°C: about 10% of maximal activity, wild-type enzyme Chloroflexus aurantiacus
55 70 55°C: about 45% of maximal activity, 70°C: about 75% of maximal activity, mutant enzyme E165Q and E165K Chloroflexus aurantiacus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
68
-
melting temperature of wild-type enzyme at pH 7.5 is 67.8°C Chloroflexus aurantiacus
75
-
half-life at pH 7.5: 0.6 min for wild-type enzyme, 228 min for mutant enzyme E165Q, 338 min for mutant enzyme E165K Chloroflexus aurantiacus
79
-
melting temperature of wild-type enzyme at pH 6.0 is 79.4°C Chloroflexus aurantiacus
80
-
melting temperature of wild-type enzyme at pH 4.4 is 80.4°C Chloroflexus aurantiacus
85
-
half-life at pH 7.5: 35 min for mutant enzyme E165Q, 46 min for mutant enzyme E165K Chloroflexus aurantiacus
85
-
melting temperature of mutant enzyme E165K at pH 4.4 Chloroflexus aurantiacus
86
-
melting temperature of mutant enzyme E165Q at pH 4.4 is 85.8°C Chloroflexus aurantiacus
91
-
melting temperature of mutant enzyme E165Q at pH 6.0 is 90.6°C, melting temperature of mutant enzyme E165Q at pH 7.5 or mutant enzyme E165K at pH 6.0 is 91.4°C Chloroflexus aurantiacus
92
-
melting temperature of mutant enzyme E165K at pH 7.5 is 91.7°C Chloroflexus aurantiacus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Chloroflexus aurantiacus
NADH
-
Chloroflexus aurantiacus