1979
DOI: 10.1016/s0021-9258(19)86571-7
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Covalent adducts of lactate oxidase. Photochemical formation and structure identification.

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Cited by 55 publications
(40 citation statements)
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“…The peak at 320 nm is more pronounced with 4 (Figure D). The decreases at 379 and 450 nm are consistent with reduction of the FAD, and the increasing feature near 320 nm is interpreted as reporting on covalent modification of the FAD N5. …”
Section: Resultssupporting
confidence: 58%
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“…The peak at 320 nm is more pronounced with 4 (Figure D). The decreases at 379 and 450 nm are consistent with reduction of the FAD, and the increasing feature near 320 nm is interpreted as reporting on covalent modification of the FAD N5. …”
Section: Resultssupporting
confidence: 58%
“…Similarly, inactivation with oxamate produced reduced FMN with carbamate bonded to the N5. In 1979, Ghisla et al further characterized analogous reactions of lactate oxidase with several mono- and dicarboxylic acids . The first in crystallo characterization of this type of reaction was done with D-amino acid oxidase and the inhibitor 3-methyl-2-oxobutyric acid; the structure showed the N5 of the reduced FAD was acylated, consistent with decarboxylation of the inhibitor (PDB ID 1DAO).…”
Section: Resultsmentioning
confidence: 99%
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