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

BRENDA support

Literature summary for 1.5.3.1 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

Inhibitors Comment Organism Structure
acetate competitive Corynebacterium sp.
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.
additional information enzyme is sensitive to SH-reagents Corynebacterium sp.

Organism

Organism UniProt Comment Textmining
Corynebacterium sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
to homogeneity Corynebacterium sp.

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
tetramer heterotetramer Corynebacterium sp.

Synonyms

Synonyms Comment Organism
SO
-
Corynebacterium sp.
SO-U96
-
Corynebacterium sp.

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

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