Literature summary extracted from

Hassan-Abdallah, A.; Zhao, G.; Jorns, M.S.
Role of the covalent flavin linkage in monomeric sarcosine oxidase (2006), Biochemistry, 45, 9454-9462.

Protein Variants

EC Number	Protein Variants	Comment	Organism
1.5.3.1	C314A	mutation of the covalent attachment site of FAD, mutant forms unstable complexes with FAD. In situ reconstitution of activity by assaying mutant in presence of FAD or 8-nor-8-chloro-FAD, giving a specific activity of 14% or 80% of wild-type, resp. Mutant exhibits high affinity for reduced flavin	Bacillus sp. (in: Bacteria)

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
1.5.3.1	5-deaza-FAD	competitive inhibition of flavinylation of apoenzyme	Bacillus sp. (in: Bacteria)

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.5.3.1	Bacillus sp. (in: Bacteria)	-	-	-

Specific Activity [micromol/min/mg]

EC Number	Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
1.5.3.1	4.1	-	pH 8.0, 25°C, mutant C315A, presence of FAD	Bacillus sp. (in: Bacteria)
1.5.3.1	23.2	-	pH 8.0, 25°C, mutant C315A, presence of 8-nor-8-chloro-FAD	Bacillus sp. (in: Bacteria)
1.5.3.1	44.8	-	pH 8.0, 25°C, native enzyme	Bacillus sp. (in: Bacteria)

Substrates and Products (Substrate)

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

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Release 2023.1 (January 2023)