The structure of the covalent flavin adduct formed between lactate oxidase and the suicide substrate 2-hydroxy-3-butynoate.

Content Provider	Semantic Scholar
Author	Schonbrunn, Agnes Walsh, Christopher T. Ghisla, Sandro Ogata, Hideaki Massey, Vickie
Copyright Year	1976
Abstract	2-Hydroxy-3-butynoic acid is a suicide substrate for Mycobacterium smegmatis lactate oxidase. Inactivation occurs by covalent modification of enzyme-bound FMN and does not involve labeling of the apoprotein. The spectrum of the enzyme bound adduct suggests that it is a 4a, 5-dihydroflavin derivative. When this adduct is released from the enzyme, a complex mixture of unstable compounds is obtained. When the initially formed enzyme-bound adduct is reduced with NaBH4, a major stable species can be resolved from the enzyme and can be isolated and purified. The structure was established by appropriate isotope substitutions. Fourier transform NMR spectroscopy, chemical reactivity, and synthesis of a model compound. The structure of the isolated adduct is structure II, Scheme II. The structure proposed for the adduct initially formed on the enzyme is structure VII, Scheme II.
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Alternate Webpage(s)	http://kops.uni-konstanz.de/bitstream/handle/123456789/7158/biochemistry_1976_schonbrunnthe_structure_of_the_covalent.pdf;jsessionid=21D16D1D27A8C3D28E9254DCA3A5E249?sequence=1
Alternate Webpage(s)	https://kops.uni-konstanz.de/bitstream/handle/123456789/7158/Biochemistry_1976_SchonbrunnThe_structure_of_the_covalent.pdf?isAllowed=y&sequence=1
PubMed reference number	1268196v1
Volume Number	15
Issue Number	9
Journal	Biochemistry
Language	English
Access Restriction	Open
Subject Keyword	2-hydroxy-3-butynoate 2-hydroxy-3-butynoic acid 4,6-dinitro-o-cresol Apoproteins Covalent Interaction Flavin Mononucleotide Isotopes Lactic acid Maxillary right second premolar abutment Mycobacterium smegmatis Unstable Medical Device Problem adduct
Content Type	Text
Resource Type	Article