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Mechanism of serine protease action. Ionization behavior of tetrahedral adduct between α-lytic protease and tripeptide aldehyde studied by carbon-13 magnetic resonance

Hunkapiller, Michael W. and Smallcombe, Stephen H. and Richards, John H. (1975) Mechanism of serine protease action. Ionization behavior of tetrahedral adduct between α-lytic protease and tripeptide aldehyde studied by carbon-13 magnetic resonance. Organic Magnetic Resonance, 7 (6). pp. 262-265. ISSN 0030-4921. http://resolver.caltech.edu/CaltechAUTHORS:20150505-151434849

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Abstract

Magnetic resonance techniques have been used to study the ionization behavior of the catalytic triad of the serine protease, α-lytic protease, in the tetrahedral, hemiacetal complex it forms with the aldehyde inhibitor, N-ac-L-ala-L-pro-L-alaninal. Chemical shift, coupling constant and relaxation measurements of a carbon-13 nucleus specifically incorporated in C-2 of the imidazole ring of the single histidine residue of the protein show that, above pH 7, the imidazole ring of the catalytic triad in the enzyme + aldehyde complex is neutral. We suggest, further, that a neutral carboxylic acid group for Asp 102 and an oxyanion for the hemiacetal are most likely to describe the state of ionization of the other groups above pH 7. Around pH 6·25, both the oxyanion and the histidine become protonated in a co-operative process which forces the histidine away from its rigidly localized position as a member of the catalytic triad into a solution-like environment.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1002/mrc.1270070604 DOIArticle
http://onlinelibrary.wiley.com/doi/10.1002/mrc.1270070604/abstractPublisherArticle
Additional Information:© 1975 Heyden & Son Limited. Received 2 December 1974; accepted 3 February 1975. Supported by grants from USPHS NIH GM 10218 and NIH GM 16424
Funders:
Funding AgencyGrant Number
NIHGM 10218
NIHGM 16424
Record Number:CaltechAUTHORS:20150505-151434849
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20150505-151434849
Official Citation:Hunkapiller, M. W., Smallcombe, S. H. and Richards, J. H. (1975), Mechanism of serine protease action. Ionization behavior of tetrahedral adduct between α-lytic protease and tripeptide aldehyde studied by carbon-13 magnetic resonance. Org. Magn. Reson., 7: 262–265. doi: 10.1002/mrc.1270070604
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:57246
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:06 May 2015 16:36
Last Modified:06 May 2015 16:36

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