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Reply to Menger and Haim (1992)

Schowen, R. L.

[s.l.] : Nature Publishing Group

Nature 360 (1992), S. 506-506

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ISSN: 1476-4687

Source: Nature Archives 1869 - 2009

Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics

Notes: [Auszug] SIR - In the 10 years or so I have done editorial work for the Journal of the American Chemical Society (JACS), I have from time to time incurred the anger of authors whose papers I felt it my duty to reject, both with and without advice from referees. One colleague threatened a lawsuit, one ...

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1038/360506a0

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The probable conformation of substrates recognized by dipeptidyl-peptidase IV and some aspects of the catalytic mechanism derived from theoretical investigations (1992)

Brandt, W. ; Lehmann, T. ; Hofmann, T. ; [et al.]

Springer

Journal of computer aided molecular design 6 (1992), S. 159-174

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ISSN: 1573-4951

Keywords: Dipeptidyl-peptidase IV ; ECEPP ; Theoretical conformational analysis ; Recognition conformation ; Catalytic mechanism

Source: Springer Online Journal Archives 1860-2000

Topics: Chemistry and Pharmacology

Notes: 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.