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Literature summary extracted from

  • Zeller, H.D.; Hille, R.; Jorns, M.S.
    Bacterial sarcosine oxidase identification of novel substrates and a biradical reaction intermediate (1989), Biochemistry, 28, 5145-5154 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.3.24 2-Furoic acid competitive inhibitor with respect to sarcosine Corynebacterium sp. P-1
1.5.3.24 2-pyrrolecarboxylic acid
-
 Corynebacterium sp. P-1

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.3.24 sarcosine + 5,6,7,8-tetrahydrofolate + O2 Corynebacterium sp. P-1
-
 glycine + 5,10-methylenetetrahydrofolate + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.5.3.24 Corynebacterium sp. P-1
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.3.24 L-2-azetidinecarboxylic acid + O2
-
 Corynebacterium sp. P-1 ?
-
 ?
1.5.3.24 L-pipecolic acid + O2
-
 Corynebacterium sp. P-1 ?
-
 ?
1.5.3.24 L-proline + O2 poor substrate, the reduction of the enzyme with L-proline at pH 8.0 is not significant under aerobic conditions Corynebacterium sp. P-1 ?
-
 ?
1.5.3.24 additional information no activity with D-proline Corynebacterium sp. P-1 ?
-
-
1.5.3.24 sarcosine + 5,6,7,8-tetrahydrofolate + O2
-
 Corynebacterium sp. P-1 glycine + 5,10-methylenetetrahydrofolate + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.5.3.24 heterotetramer 1 * 100000 + 1 * 42000 + 1 * 20000 + 1 * 6000, SDS-PAGE Corynebacterium sp. P-1

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.3.24 FAD the enzyme contains both covalently bound FAD [8a-(7V3-histidyl)FAD] and noncovalently bound FAD Corynebacterium sp. P-1

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.5.3.24 0.14
-
 2-Furoic acid pH and temperature not specified in the publication Corynebacterium sp. P-1