Enzymological characteristics of a novel archaeal dye-linked d-lactate dehydrogenase showing loose binding of FAD-Reference-Cited by-同舟云学术

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Enzymological characteristics of a novel archaeal dye-linked d-lactate dehydrogenase showing loose binding of FAD

Published:2018-09-11 Issue:6 Volume:22 Page:975-981
ISSN:1431-0651
Container-title:Extremophiles
language:en
Short-container-title:Extremophiles

Author:

Satomura Takenori,Hayashi Junji,Ohshida Tatsuya,Sakuraba Haruhiko,Ohshima Toshihisa,Suye Shin-ichiro

Publisher

Springer Science and Business Media LLC

Subject

Molecular Medicine,General Medicine,Microbiology

Link

http://link.springer.com/article/10.1007/s00792-018-1054-3/fulltext.html

Reference19 articles.

1. Brizio C, Galluccio M, Wait R, Torchetti EM, Bafunno V, Accardi R, Gianazzae E, Indiverib C, Barile M (2006) Over-expression in Escherichia coli and characterization of two recombinant isoforms of human FAD synthetase. Biochem Biophys Res Commun 344:1008–1016. https://doi.org/10.1016/j.bbrc.2006.04.003

2. Brockman HL, Wood WA (1975) d-Lactate dehydrogenase of Peptostreptococcus elsdenii. Methods Enzymol 41:309–312. https://doi.org/10.1016/S0076-6879(75)41070-9

3. Dym O, Pratt EA, Ho C, Eisenberg D (2000) The crystal structure of d-lactate dehydrogenase, a peripheral membrane respiratory enzyme. Proc Natl Acad Sci USA 97:9413–9418. https://doi.org/10.1073/pnas.97.17.9413

4. Frew JE, Hill HA (1987) Electrochemical biosensors. Anal Chem 59:933A–944A. https://doi.org/10.1021/ac00142a720

5. Gregolin C, Singer TP (1963) The lactic dehydrogenase of yeast. III. d(−)Lactic cytochrome c reductase, a zinc flavoprotein from aerobic yeast. Biochim Biophys Acta 67:201–218. https://doi.org/10.1016/0926-6569(63)90229-3

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