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Literature summary extracted from

  • Mukouyama, E.B.; Oguchi, M.; Kodera, Y.; Maeda, T.; Suzuki, H.
    Low pKa lysine residues at the active site of sarcosine oxidase from Corynebacterium sp. U-96 (2004), Biochem. Biophys. Res. Commun., 320, 846-851.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.3.1 acetate competitive Corynebacterium sp.
1.5.3.1 iodoacetamide inactivation by modification of 2 specific lysine residues, one of which is Lys358, pH-depedency of inactivation in presence and absence of competitive inhibitor acetate lowerig the pKa for the epsilon-amino groups, inactivation kinetics at different pH-values Corynebacterium sp.
1.5.3.1 additional information enzyme is sensitive to SH-reagents Corynebacterium sp.

Organism

EC Number Organism UniProt Comment Textmining
1.5.3.1 Corynebacterium sp.
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.3.1 to homogeneity Corynebacterium sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.3.1 sarcosine + H2O + O2
-
 Corynebacterium sp. glycine + formaldehyde + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.5.3.1 tetramer heterotetramer Corynebacterium sp.

Synonyms

EC Number Synonyms Comment Organism
1.5.3.1 SO
-
 Corynebacterium sp.
1.5.3.1 SO-U96
-
 Corynebacterium sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.3.1 25
-
 assay at Corynebacterium sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.3.1 8
-
 assay at Corynebacterium sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.3.1 FAD noncovalently bound Corynebacterium sp.
1.5.3.1 FMN 1 molecle covalently bound to the tetrameric enzyme Corynebacterium sp.
1.5.3.1 NAD+
-
 Corynebacterium sp.