caa a22 4500 469053267 CHVBK 20180323132836.0 cr unu---uuuuu 170328e19920201xx s 000 0 eng 10.1007/BF00124383 doi (NATIONALLICENCE)springer-10.1007/BF00124383 A prediction of the three-dimensional structure of maize NADP+-dependent malate dehydrogenase which explains aspects of light-dependent regulation unique to plant enzymes [Elektronische Daten] [Richard Jackson, Richard Sessions, J. Holbrook] Summary: A model has been built for the plant NADP-malate dehydrogenase from Zea mays, a key enzyme in photosynthesis, which undergoes light-dependent regulation. The model was based on sequence and presumed structural homology to the known three-dimensional structure of mammalian porcine cytosolic NAD-malate dehydrogenase. A cystine-loop present in an extended C-terminal region of plant NADP-malate dehydrogenases was modelled using molecular mechanics and computer graphical methods, based on the assumption that a disulphide bridge exists in the inactive form of the enzyme between Cys351 and Cys363. The predicted conformation of the intact C-terminal cystine-loop suggests that the extended polypeptide will bind in the active centre and inhibit enzyme activity. Another ionizable cysteine residue in the active site is predicted to control the charge of the catalytic His215 and might be responsible for the uniquely tight binding of the positively charged nicotinamide ring of NADP+ in this and other C4 and C3 plant NADP-malate dehydrogenases. ESCOM Science Publishers B.V, 1992 NADP-malate dehydrogenase nationallicence Molecular model nationallicence C-terminal cystine loop nationallicence C-terminal ‘internal inhibitor' nationallicence Active site cysteine nationallicence Jackson Richard Molecular Recognition Centre, University of Bristol School of Medical Sciences, University Walk, BS8 1TD, Bristol, U.K. aut Sessions Richard Molecular Recognition Centre, University of Bristol School of Medical Sciences, University Walk, BS8 1TD, Bristol, U.K. aut Holbrook J. Molecular Recognition Centre, University of Bristol School of Medical Sciences, University Walk, BS8 1TD, Bristol, U.K. aut Journal of Computer-Aided Molecular Design Kluwer Academic Publishers 6/1(1992-02-01), 1-18 0920-654X 6:1<1 1992 6 10822 https://doi.org/10.1007/BF00124383 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00124383 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Jackson Richard Molecular Recognition Centre, University of Bristol School of Medical Sciences, University Walk, BS8 1TD, Bristol, U.K aut NATIONALLICENCE 700 1- Sessions Richard Molecular Recognition Centre, University of Bristol School of Medical Sciences, University Walk, BS8 1TD, Bristol, U.K aut NATIONALLICENCE 700 1- Holbrook J. Molecular Recognition Centre, University of Bristol School of Medical Sciences, University Walk, BS8 1TD, Bristol, U.K aut NATIONALLICENCE 773 0- Journal of Computer-Aided Molecular Design Kluwer Academic Publishers 6/1(1992-02-01), 1-18 0920-654X 6:1<1 1992 6 10822 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer