Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Sullivan, P.A.; Soon, C.Y.; Schreurs, W.J.; Cutfield, J.F.; Sheperd, M.G.
    The structure of L-lactate oxidase from Mycobacterium smegmatis (1977), Biochem. J., 165, 375-383.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.13.12.4
-
 Mycolicibacterium smegmatis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.13.12.4 43655
-
 8 * 43655, amino acid analysis, per mol of FMN Mycolicibacterium smegmatis
1.13.12.4 345000
-
 sedimentation-equilibrium analysis Mycolicibacterium smegmatis

Organism

EC Number Organism UniProt Comment Textmining
1.13.12.4 Mycolicibacterium smegmatis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.12.4
-
 Mycolicibacterium smegmatis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.13.12.4 53.6
-
-
 Mycolicibacterium smegmatis

Storage Stability

EC Number Storage Stability Organism
1.13.12.4 0°C, crystalline suspension at 2-10 mg per ml for at least 6 months without loss of activity in the dark Mycolicibacterium smegmatis

Subunits

EC Number Subunits Comment Organism
1.13.12.4 octamer 8 * 43655, amino acid analysis, per mol of FMN Mycolicibacterium smegmatis

Cofactor

EC Number Cofactor Comment Organism Structure
1.13.12.4 FMN
-
 Mycolicibacterium smegmatis