Literature summary for 1.5.3.1 extracted from

Hassan-Abdallah, A.; Zhao, G.; Jorns, M.S.
Covalent flavinylation of monomeric sarcosine oxidase: identification of a residue essential for holoenzyme biosynthesis (2008), Biochemistry, 47, 1136-1143.

Search for more literature for 1.5.3.1

Cloned(Commentary)

Cloned (Comment)	Organism
native and mutant enzyme in Escherichia coli BL21(DE3), R49 mutants contain His-tag	Bacillus sp. (in: Bacteria)

Protein Variants

Protein Variants	Comment	Organism
C315A	inactive, no bound FAD, forms stable non-covalent complex with 5-deazaFAD	Bacillus sp. (in: Bacteria)
H45A	contains covalently bound FAD, 4fold less FAD than in wild type enzyme, catalytic properties similar than wild type enzyme, 50% of wild type activity	Bacillus sp. (in: Bacteria)
H45N	contains covalently bound FAD, 4fold less FAD than in wild type enzyme, catalytic properties similar than wild type enzyme, 50% of wild type activity	Bacillus sp. (in: Bacteria)
R49A	inactive, no bound FAD, forms stable non-covalent complex with 5-deazaFAD	Bacillus sp. (in: Bacteria)
R49K	contains covalently bound FAD, 4fold less FAD than in wild type enzyme, 4% of wild type activity	Bacillus sp. (in: Bacteria)
R49Q	inactive	Bacillus sp. (in: Bacteria)

Organism

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

Purification (Commentary)

Purification (Comment)	Organism
recombinant proteins	Bacillus sp. (in: Bacteria)

Synonyms

Synonyms	Comment	Organism
monomeric sarcosine oxidase	-	Bacillus sp. (in: Bacteria)
MSOX	-	Bacillus sp. (in: Bacteria)

Cofactor

Cofactor	Comment	Organism	Structure
FAD	covalently bound	Bacillus sp. (in: Bacteria)

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Release 2023.1 (January 2023)