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PMID: 16592059 Published · ppublish English Journal Article

Influence of Leaving-Group Electronic Effect on alpha-Chymotrypsin: Catalytic Constants of Specific Substrates.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 70 ·No. 2 ·1973-02-00 ·Pages 517-20

Philipp M, Pollack RM, Bender ML

Abstract

Rate constants and binding constants for the alpha-chymotrypsin-catalyzed hydrolysis of N-acetyltyrosine, tryptophan, and phenylalanine anilides are presented. Both k(cat) and K(m) are independent of electronic effects in the substrate over a range of 9.8 orders of magnitude (as measured by pK of the leaving group). Similarly, K(m) is independent of charge and orientation about the alpha-carbon for various substrates and pseudo-substrates. These results are not consistent with the pretransition state protonation hypothesis; instead, they are discussed in terms of a tetrahedral intermediate that is thermodynamically less stable than the Michaelis complex.

Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Philipp M
Department of Chemistry, Northwestern University, Evanston, Illinois 60201.
Pollack R M
Bender M L
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22 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.70.2.517
Published
1973-02-00
Pages
517-20
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC433295
External Links
PubMed source DOI: 10.1073/pnas.70.2.517 PMC Full Text View journal details
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