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• W2033480762 abstract "Heterotetrameric (αβγδ) sarcosine oxidase from Corynebacterium sp. P-1 (cTSOX) contains noncovalently bound FAD and NAD+ and covalently bound FMN, attached to β(His173). The β(His173Asn) mutant is expressed as a catalytically inactive, labile heterotetramer. The β and δ subunits are lost during mutant enzyme purification, which yields a stable αγ complex. Addition of stabilizing agents prevents loss of the δ but not the β subunit. The covalent flavin link is clearly a critical structural element and essential for TSOX activity or preventing FMN loss. The α subunit was expressed by itself and purified by affinity chromatography. The α and β subunits each contain an NH2-terminal ADP-binding motif that could serve as part of the binding site for NAD+ or FAD. The α subunit and the αγ complex were each found to contain 1 mol of NAD+ but no FAD. Since NAD+ binds to α, FAD probably binds to β. The latter could not be directly demonstrated since it was not possible to express β by itself. However, FAD in TSOX from Pseudomonas maltophilia (pTSOX) exhibits properties similar to those observed for the covalently bound FAD in monomeric sarcosine oxidase and N-methyltryptophan oxidase, enzymes that exhibit sequence homology with β. A highly conserved glycine in the ADP-binding motif of the α(Gly139) or β(Gly30) subunit was mutated in an attempt to generate NAD+- or FAD-free cTSOX, respectively. The α(Gly139Ala) mutant is expressed only at low temperature (toptimum = 15 °C), but the purified enzyme exhibited properties indistinguishable from the wild-type enzyme. The much larger barrier to NAD+ binding in the case of the α(Gly139Val) mutant could not be overcome even by growth at 3 °C, suggesting that NAD+ binding is required for TSOX expression. The β(Gly30Ala) mutant exhibited subunit expression levels similar to those of the wild-type enzyme, but the mutation blocked subunit assembly and covalent attachment of FMN, suggesting that both processes require a conformational change in β that is induced upon FAD binding. About half of the covalent FMN in recombinant preparations of cTSOX or pTSOX is present as a reversible covalent 4a-adduct with a cysteine residue. Adduct formation is not prevented by mutating any of the three cysteine residues in the β subunit of cTSOX to Ser or Ala. Since FMN is attached via its 8-methyl group to the β subunit, the FMN ring must be located at the interface between β and another subunit that contains the reactive cysteine residue." @default.
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• W2033480762 date "2001-04-13" @default.
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• W2033480762 title "Organization of the Multiple Coenzymes and Subunits and Role of the Covalent Flavin Link in the Complex Heterotetrameric Sarcosine Oxidase" @default.
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• W2033480762 doi "https://doi.org/10.1021/bi010101p" @default.
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