Perediction of Secondary Structural Elements in Glycerol-3-Phosphate Dehydrogenase by Comparison with Other Dehydrogenases
1980; Wiley; Volume: 109; Issue: 2 Linguagem: Inglês
10.1111/j.1432-1033.1980.tb04798.x
ISSN1432-1033
AutoresJoachim Otto, Patrick Argos, Michael G. Rossmann,
Tópico(s)Advanced Proteomics Techniques and Applications
ResumoEuropean Journal of BiochemistryVolume 109, Issue 2 p. 325-330 Free Access Perediction of Secondary Structural Elements in Glycerol-3-Phosphate Dehydrogenase by Comparison with Other Dehydrogenases Joachim OTTO, Joachim OTTO Institut für Physiologische Chemie, Physikalische Biochemie und Zellbiologie, Ludwig-Maximilians-Universität München, Goethestraße 33, D-8000 München 2, Federal Republic of GermanySearch for more papers by this authorPatrick ARGOS, Patrick ARGOS Department of Biological Sciences, Purdue University West Lafayette, Indiana 47907, USASearch for more papers by this authorMichael G. ROSSMANN, Michael G. ROSSMANN Department of Biological Sciences, Purdue University West Lafayette, Indiana 47907, USASearch for more papers by this author Joachim OTTO, Joachim OTTO Institut für Physiologische Chemie, Physikalische Biochemie und Zellbiologie, Ludwig-Maximilians-Universität München, Goethestraße 33, D-8000 München 2, Federal Republic of GermanySearch for more papers by this authorPatrick ARGOS, Patrick ARGOS Department of Biological Sciences, Purdue University West Lafayette, Indiana 47907, USASearch for more papers by this authorMichael G. ROSSMANN, Michael G. ROSSMANN Department of Biological Sciences, Purdue University West Lafayette, Indiana 47907, USASearch for more papers by this author First published: August 1980 https://doi.org/10.1111/j.1432-1033.1980.tb04798.xCitations: 52AboutSectionsPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Abstract The secondary structure of glycerol-3-phosphate dehydrogenase was predicted from its amino acid sequence. The pattern of helices and sheets within the first half of the polypeptide as well as specific marker residues were consistent with the properties of the NAD binding domain in other dehydrogenases. The second half of the sequence shows similarities with the catalytic domain of glyceraldehyde-3-phosphate dehydrogenase. The resulting two-domain structure of glycerol-3-phos-phate dehydrogenase allows the correct environment for the B specificity of the nicotinamide ring and the L-glycerol 3-phosphate substrate. Enzymes Glycerol-3-phosphate dehydrogenase (EC 1.1.1.8) glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) lactate dehydrogenase (EC 1.1.1.27) alcohol dehydrogenase (EC 1.1.1.1) malate dehydrogenase (EC 1.1.1.37) REFERENCES 1 Rossmann, M. G., Liljas, A., Brändén, C. I. & Banaszak, L. J. (1975) in The Enzymes ( P. D. Boyer, ed.) 3rd edn, vol. XI, pp. 61– 102, Academic Press, New York . CrossrefGoogle Scholar 2 Wootton, J. C. (1974) Nature (Lond.) 252, 542– 546. 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