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Literature summary extracted from

  • Madern, D.; Ebel, C.; Dale, H.A.; Lien, T.; Steen, I.H.; Birkeland, N.K.; Zaccai, G.
    Differences in the oligomeric states of the LDH-like L-MalDH from the hyperthermophilic archaea Methanococcus jannaschii and Archaeoglobus fulgidus (2001), Biochemistry, 40, 10310-10306.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.375 expression in Escherichia coli Methanocaldococcus jannaschii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.375 57000
-
 sedimentation analysis Archaeoglobus fulgidus
1.1.1.375 113000
-
 sedimentation analysis Methanocaldococcus jannaschii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.375 (S)-malate + NAD+ Methanocaldococcus jannaschii
-
 oxaloacetate + NADH + H+
-
 ?
1.1.1.375 (S)-malate + NAD+ Archaeoglobus fulgidus
-
 oxaloacetate + NADH + H+
-
 ?
1.1.1.375 (S)-malate + NAD+ Methanocaldococcus jannaschii DSM 2661
-
 oxaloacetate + NADH + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.375 Archaeoglobus fulgidus O08349
-
-
1.1.1.375 Methanocaldococcus jannaschii Q60176
-
-
1.1.1.375 Methanocaldococcus jannaschii DSM 2661 Q60176
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.375
-
 Methanocaldococcus jannaschii
1.1.1.375
-
 Archaeoglobus fulgidus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.375 (S)-malate + NAD+
-
 Methanocaldococcus jannaschii oxaloacetate + NADH + H+
-
 ?
1.1.1.375 (S)-malate + NAD+
-
 Archaeoglobus fulgidus oxaloacetate + NADH + H+
-
 ?
1.1.1.375 (S)-malate + NAD+
-
 Methanocaldococcus jannaschii DSM 2661 oxaloacetate + NADH + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.375 dimer the effects of high temperature, cofactor binding, and high phosphate concentration are studied. They do not modify the oligomeric state of the enzyme. Enzymatic activity of the dimeric enzyme is controlled by a pH-dependent transition at pH 7 without dissociation of the subunits Archaeoglobus fulgidus
1.1.1.375 tetramer the effects of high temperature, cofactor binding, and high phosphate concentration are studied. They do not modify the oligomeric state of the enzyme Methanocaldococcus jannaschii

Synonyms

EC Number Synonyms Comment Organism
1.1.1.375 LDH-like L-MalDH
-
 Methanocaldococcus jannaschii
1.1.1.375 LDH-like L-MalDH
-
 Archaeoglobus fulgidus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.375 70
-
 assay at Archaeoglobus fulgidus
1.1.1.375 80
-
 assay at Methanocaldococcus jannaschii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.375 8
-
 assay at Methanocaldococcus jannaschii
1.1.1.375 8
-
 assay at Archaeoglobus fulgidus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.375 7
-
 enzymatic activity of the dimeric enzyme is controlled by a pH-dependent transition between an active and inactive dimeric state at pH 7 without dissociation of the subunits Archaeoglobus fulgidus