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Literature summary for 1.1.5.4 extracted from

  • Imai, K.; Brodie, A.F.
    A phospholipid-requiring enzyme, malate-vitamin K reductase (1973), J. Biol. Chem., 248, 7487-7494.
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
Phospholipid activity of purified enzyme is dependent on added phospholipid Mycolicibacterium phlei

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
51000
-
1 * 51000, at high salt concentrations the enzyme exists as a monomeric form which is more active than the aggregated form, SDS-PAGE Mycolicibacterium phlei
53000
-
monomeric enzyme form, gel filtration Mycolicibacterium phlei
164000
-
aggregated form, gel filtration Mycolicibacterium phlei

Organism

Organism UniProt Comment Textmining
Mycolicibacterium phlei
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Mycolicibacterium phlei

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
52
-
-
Mycolicibacterium phlei

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-malate + vitamin K1
-
Mycolicibacterium phlei oxaloacetate + reduced vitamin K1
-
?

Subunits

Subunits Comment Organism
monomer 1 * 51000, at high salt concentrations the enzyme exists as a monomeric form which is more active than the aggregated form, SDS-PAGE Mycolicibacterium phlei

Synonyms

Synonyms Comment Organism
malate-vitamin K reductase
-
Mycolicibacterium phlei

Cofactor

Cofactor Comment Organism Structure
FAD the enzyme requires FAD and vitamin K for activity Mycolicibacterium phlei
additional information no spectral evidence for the presence of a flavin or quinone in the purified enzyme Mycolicibacterium phlei
vitamin K1 the enzyme requires FAD and vitamin K for activity Mycolicibacterium phlei