Book chapter
Interaction of bacterial sarcosine oxidase with folate derivatives
Flavins and Flavoproteins 1987, pp 713-716
31 Dec 1987
Abstract
Sarcosine oxidase from Corynebacterium sp. P-l contains both covalently bound FAD [8o-(N3-histidyl)-FAD] and noncovalently bound FAD. The enzyme is composed of 4 nonidentical subunits (Mr, 100,000, 42,000, 20,000 and 6,000). This unusual subunit composition is a genuine property of the enzyme and not a proteolytic artifact (1). A similar sarcosine oxidase has been isolated from Corynebacterium sp. U-96 (1-3). The presence of both covalent and noncovalent flavin distinguishes these enzymes from all other known flavoproteins. Their complex quaternary structure is also unique as compared with other sarcosine oxidizing enzymes. Mammalian sarcosine dehydrogenase is a monomeric protein, containing only covalently bound flavin (4-6). That the mammalian enzyme has a catalytically significant binding site for tetrahydrofolate (H4folate) (7,8) prompted studies (9) to determine whether a similar property might be observed with a more complex bacterial enzyme.
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Details
- Title
- Interaction of bacterial sarcosine oxidase with folate derivatives
- Creators
- Marilyn Schuman Jörns - Drexel University, Hahnemann University (1982-1993)Kalla Kvalnes-Krick - Drexel University, Hahnemann University (1982-1993)
- Publication Details
- Flavins and Flavoproteins 1987, pp 713-716
- Conference
- Flavins and Flavoproteins 1987 : the Ninth International Symposium, 9th (Atlanta, Georgia, United States, 07 Jun 1987–12 Jun 1987)
- Publisher
- De Gruyter; Berlin, Boston
- Number of pages
- 4
- Resource Type
- Book chapter
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Other Identifier
- 991020545410004721