caa a22 4500 469053755 CHVBK 20180323132837.0 cr unu---uuuuu 170328e19920401xx s 000 0 eng 10.1007/BF00129426 doi (NATIONALLICENCE)springer-10.1007/BF00129426 The probable conformation of substrates recognized by dipeptidyl-peptidase IV and some aspects of the catalytic mechanism derived from theoretical investigations [Elektronische Daten] [W. Brandt, T. Lehmann, T. Hofmann, R. Schowen, A. Barth] Summary: By theoretical conformational investigations of substrates and nonsubstrates of the enzyme dipeptidyl-peptidase IV (DP IV) as well as dipeptide-esters using the ECEPP83 method we determined the structure of peptides recognized and cleaved by the enzyme. From a comparison of all possible structures for the substrates with conformations not possible in nonsubstrates we concluded that a single conformation explains substrate specificities of DP IV. This conformation is characterized by the following dihedral angles: {ie159-1}, {ie159-2}, {ie159-3}, {ie159-4}, and {ie159-5}. The conclusions were supported by comparisons of molecular electrostatic potentials calculated with the molecular graphics program HAMOG. ESCOM Science Publishers B.V, 1992 Dipeptidyl-peptidase IV nationallicence ECEPP nationallicence Theoretical conformational analysis nationallicence Recognition conformation nationallicence Catalytic mechanism nationallicence Brandt W. Institute of Biochemistry, Martin-Luther-University Halle-Wittenberg, Weinbergweg 16a, Halle/Saale, Germany aut Lehmann T. Institute of Biochemistry, Martin-Luther-University Halle-Wittenberg, Weinbergweg 16a, Halle/Saale, Germany aut Hofmann T. Institute of Biochemistry, Martin-Luther-University Halle-Wittenberg, Weinbergweg 16a, Halle/Saale, Germany aut Schowen R. Department of Chemistry, University of Kansas, 66045-0046, Lawrence, KS, U.S.A. aut Barth A. Institute of Biochemistry, Martin-Luther-University Halle-Wittenberg, Weinbergweg 16a, Halle/Saale, Germany aut Journal of Computer-Aided Molecular Design Kluwer Academic Publishers 6/2(1992-04-01), 159-174 0920-654X 6:2<159 1992 6 10822 https://doi.org/10.1007/BF00129426 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00129426 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Brandt W. Institute of Biochemistry, Martin-Luther-University Halle-Wittenberg, Weinbergweg 16a, Halle/Saale, Germany aut NATIONALLICENCE 700 1- Lehmann T. Institute of Biochemistry, Martin-Luther-University Halle-Wittenberg, Weinbergweg 16a, Halle/Saale, Germany aut NATIONALLICENCE 700 1- Hofmann T. Institute of Biochemistry, Martin-Luther-University Halle-Wittenberg, Weinbergweg 16a, Halle/Saale, Germany aut NATIONALLICENCE 700 1- Schowen R. Department of Chemistry, University of Kansas, 66045-0046, Lawrence, KS, U.S.A aut NATIONALLICENCE 700 1- Barth A. Institute of Biochemistry, Martin-Luther-University Halle-Wittenberg, Weinbergweg 16a, Halle/Saale, Germany aut NATIONALLICENCE 773 0- Journal of Computer-Aided Molecular Design Kluwer Academic Publishers 6/2(1992-04-01), 159-174 0920-654X 6:2<159 1992 6 10822 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer