Literature DB >> 4758115

A molecular orbital study on the enzymic reaction mechanism of alpha-chymotrypsin.

H Umeyama, A Imamura, C Nagata.   

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Year:  1973        PMID： 4758115     DOI： 10.1016/0022-5193(73)90057-x

Source DB:  PubMed          Journal:  J Theor Biol        ISSN： 0022-5193            Impact factor:   2.691


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  5 in total

1.  Molecular orbital studies of enzyme activity: I: Charge relay system and tetrahedral intermediate in acylation of serine proteinases.

Authors:  S Scheiner; D A Kleier; W N Lipscomb
Journal:  Proc Natl Acad Sci U S A       Date:  1975-07       Impact factor: 11.205

2.  Enzymes work by solvation substitution rather than by desolvation.

Authors:  A Warshel; J Aqvist; S Creighton
Journal:  Proc Natl Acad Sci U S A       Date:  1989-08       Impact factor: 11.205

3.  Charge state of His-57-Asp-102 couple in a transition state analogue-trypsin complex: a molecular orbital study.

Authors:  H Umeyama; S Hirono; S Nakagawa
Journal:  Proc Natl Acad Sci U S A       Date:  1984-10       Impact factor: 11.205

4.  Catalytic reaction mechanism of acetylcholinesterase determined by Born-Oppenheimer ab initio QM/MM molecular dynamics simulations.

Authors:  Yanzi Zhou; Shenglong Wang; Yingkai Zhang
Journal:  J Phys Chem B       Date:  2010-07-08       Impact factor: 2.991

5.  Stereoelectronic control in peptide bond formation. Ab initio calculations and speculations on the mechanism of action of serine proteases.

Authors:  D G Gorenstein; K Taira
Journal:  Biophys J       Date:  1984-12       Impact factor: 4.033
  5 in total

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