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Literature summary for 1.1.1.375 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
Search for more literature for 1.1.1.375

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Methanocaldococcus jannaschii

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

Purification (Comment) Organism
-
 Methanocaldococcus jannaschii
-
 Archaeoglobus fulgidus

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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
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

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

Temperature Optimum [°C]

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

pH Optimum

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

pH Range

pH Minimum pH Maximum Comment Organism
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