Abstract
A number of authors have reported observations on D-amino acid oxidase [D-amino acid: O2 oxidoreductase (deaminating), EC 1.4.3.3.] that they have interpreted in terms of a temperature-dependent conformational transition having a van't Hoff enthalpy amounting to more than 1 cal per g of protein (1 cal = 4.184J). No indication of this transition is obtained by using a differential scanning calorimeter having a sensitivity considerably in excess of that required to detect such a transition. The implications of this discrepancy are discussed.
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Selected References
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- Antonini E., Brunori M., Bruzzesi R., Chiancone E., Massey V. Association-dissociation phenomena of D-amino acid oxidase. J Biol Chem. 1966 May 25;241(10):2358–2366. [PubMed] [Google Scholar]
- Henn S. W., Ackers G. K. Molecular sieve studies of interacting protein systems. V. Association of subunits of D-amino acid oxidase apoenzyme. Biochemistry. 1969 Sep;8(9):3829–3838. doi: 10.1021/bi00837a049. [DOI] [PubMed] [Google Scholar]
- Kelly R. C., von Hippel P. H. DNA "melting" proteins. III. Fluorescence "mapping" of the nucleic acid binding site of bacteriophage T4 gene 32-protein. J Biol Chem. 1976 Nov 25;251(22):7229–7239. [PubMed] [Google Scholar]
- Koster J. F., Veeger C. The relation between temperature-inducible allosteric effects and the activation energies of amino-acid oxidases. Biochim Biophys Acta. 1968 Aug 27;167(1):48–63. doi: 10.1016/0005-2744(68)90276-3. [DOI] [PubMed] [Google Scholar]
- Massey V., Curti B., Ganther H. A temperature-dependent conformational change in D-amino acid oxidase and its effect on catalysis. J Biol Chem. 1966 May 25;241(10):2347–2357. [PubMed] [Google Scholar]
- Mateo P. L., Sturtevant J. M. Thermodynamics of the binding of flavin adenine dinucleotide to D-amino acid oxidase. Biosystems. 1977 Apr;8(4):247–253. doi: 10.1016/0303-2647(77)90050-8. [DOI] [PubMed] [Google Scholar]
- Privalov P. L., Khechinashvili N. N. A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. J Mol Biol. 1974 Jul 5;86(3):665–684. doi: 10.1016/0022-2836(74)90188-0. [DOI] [PubMed] [Google Scholar]
- Shiga K., Shiga T. The kinetic features of monomers and dimers in high- and low-temperature conformational states of D-amino acid oxidase. Biochim Biophys Acta. 1972 Apr 15;263(2):294–303. doi: 10.1016/0005-2795(72)90082-7. [DOI] [PubMed] [Google Scholar]
- Sturtevant J. M. Some applications of calorimetry in biochemistry and biology. Annu Rev Biophys Bioeng. 1974;3(0):35–51. doi: 10.1146/annurev.bb.03.060174.000343. [DOI] [PubMed] [Google Scholar]
- Tsong T. Y., Hearn R. P., Wrathall D. P., Sturtevant J. M. A calorimetric study of thermally induced conformational transitions of ribonuclease A and certain of its derivatives. Biochemistry. 1970 Jun 23;9(13):2666–2677. doi: 10.1021/bi00815a015. [DOI] [PubMed] [Google Scholar]
- Tu S. C., McCormick D. B. Photoinactivation of porcine D-amino acid oxidase with flavin adenine dinucleotide. J Biol Chem. 1973 Sep 25;248(18):6339–6347. [PubMed] [Google Scholar]