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Literature summary for 1.1.1.37 extracted from

  • Lee, D.; Hong, J.; Kim, K.J.
    Crystal structure and biochemical characterization of malate dehydrogenase from Metallosphaera sedula (2019), Biochem. Biophys. Res. Commun., 509, 833-838 .
    View publication on PubMed
Search for more literature for 1.1.1.37

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 (DE3)-T1R cells Metallosphaera sedula

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme in complex with NAD+, hanging drop vapor diffusion method, using 35% (v/v) 2-ethoxyethanol and 0.1M sodium cacodylate/hydrochloric acid pH 6.0 at 20°C.Enzyme as ternary complex with malate and NAD+, hanging drop vapor diffusion method, using 40% (w/v) polyethylene glycol 300, 0.1M CHES/sodium hydroxide pH 9.5, and 0.2 M sodium chloride Metallosphaera sedula

Protein Variants

Protein Variants Comment Organism
E145A the mutant shows severely reduced activity compared to the wild type enzyme Metallosphaera sedula
H172A the mutant shows severely reduced activity compared to the wild type enzyme Metallosphaera sedula
N120A the mutant shows severely reduced activity compared to the wild type enzyme Metallosphaera sedula
R148A the mutant shows severely reduced activity compared to the wild type enzyme Metallosphaera sedula
R82A the mutant shows severely reduced activity compared to the wild type enzyme Metallosphaera sedula
R88A the mutant shows severely reduced activity compared to the wild type enzyme Metallosphaera sedula
T218A the mutant shows severely reduced activity compared to the wild type enzyme Metallosphaera sedula

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.123
-
 NADH at pH 7.0, temperature not specified in the publication Metallosphaera sedula
0.165
-
 NADPH at pH 7.0, temperature not specified in the publication Metallosphaera sedula

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
133000
-
 gel filtration Metallosphaera sedula

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-malate + NAD+ Metallosphaera sedula
-
 oxaloacetate + NADH + H+
-
 r
(S)-malate + NADP+ Metallosphaera sedula
-
 oxaloacetate + NADPH + H+
-
 r
oxaloacetate + NADH + H+ Metallosphaera sedula
-
 (S)-malate + NAD+
-
 r
oxaloacetate + NADPH + H+ Metallosphaera sedula
-
 (S)-malate + NADP+
-
 r

Organism

Organism UniProt Comment Textmining
Metallosphaera sedula A0A088E2H7
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA agarose column chromatography and Sephacryl S-300 gel filtration Metallosphaera sedula

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-malate + NAD+
-
 Metallosphaera sedula oxaloacetate + NADH + H+
-
 r
(S)-malate + NADP+
-
 Metallosphaera sedula oxaloacetate + NADPH + H+
-
 r
oxaloacetate + NADH + H+
-
 Metallosphaera sedula (S)-malate + NAD+
-
 r
oxaloacetate + NADPH + H+
-
 Metallosphaera sedula (S)-malate + NADP+
-
 r

Subunits

Subunits Comment Organism
homotetramer
-
 Metallosphaera sedula

Synonyms

Synonyms Comment Organism
MDH
-
 Metallosphaera sedula

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.01
-
 NADPH at pH 7.0, temperature not specified in the publication Metallosphaera sedula
0.02
-
 NADH at pH 7.0, temperature not specified in the publication Metallosphaera sedula

Cofactor

Cofactor Comment Organism Structure
NAD+ the enzyme has a slightly higher affinity for NADH than for NADPH but can use both as cofactor Metallosphaera sedula
NADP+ the enzyme has a slightly higher affinity for NADH than for NADPH but can use both as cofactor Metallosphaera sedula