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Literature summary for 1.18.1.3 extracted from

  • Zanno, A.; Kwiatkowski, N.; Vaz, A.D.; Guardiola-Diaz, H.M.
    MT FdR: a ferredoxin reductase from M. tuberculosis that couples to MT CYP51 (2005), Biochim. Biophys. Acta, 1707, 157-169.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli MV1304 as GST-fusion protein Mycobacterium tuberculosis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43000
-
x * 69000, SDS-PAGE, GST-fusion protein, x * 43000, SDS-PAGE, native protein Mycobacterium tuberculosis
69000
-
x * 69000, SDS-PAGE, GST-fusion protein, x * 43000, SDS-PAGE, native protein Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
oxidized ferredoxin + NADH Mycobacterium tuberculosis required for activity of CYP101 reduced ferredoxin + NAD+
-
?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oxidized ferredoxin + NADH
-
Mycobacterium tuberculosis reduced ferredoxin + NAD+
-
?
oxidized ferredoxin + NADH required for activity of CYP101 Mycobacterium tuberculosis reduced ferredoxin + NAD+
-
?
oxidized ferredoxin + NADPH
-
Mycobacterium tuberculosis reduced ferredoxin + NADP+
-
?

Subunits

Subunits Comment Organism
? x * 69000, SDS-PAGE, GST-fusion protein, x * 43000, SDS-PAGE, native protein Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
FdR
-
Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
FAD associated to enzyme, 0.6-0.8 FAD per protein monomer Mycobacterium tuberculosis
NADH preferred cofactor Mycobacterium tuberculosis
NADPH much less effective cofactor than NADH Mycobacterium tuberculosis