A CONCLUDING SPECIFICATION OF THE DIMENSIONS OF THE ACTIVE-SITE MODELOF PIG-LIVER ESTERASE

Authors
PROVENCHER L JONES JB
Citation
L. Provencher et Jb. Jones, A CONCLUDING SPECIFICATION OF THE DIMENSIONS OF THE ACTIVE-SITE MODELOF PIG-LIVER ESTERASE, Journal of organic chemistry, 59(10), 1994, pp. 2729-2732
Citations number
38
Categorie Soggetti
Chemistry Inorganic & Nuclear
Journal title
Journal of organic chemistry → ACNP
ISSN journal
00223263
Volume
59
Issue
10
Year of publication
1994
Pages
2729 - 2732
Database
ISI
SICI code
0022-3263(1994)59:10<2729:ACSOTD>2.0.ZU;2-3
Abstract
Using bicyclononyl-, (adamantylmethyl)-, and biphenylmalonate substrat e probes, the dimensions of the large hydrophobic pocket of the active site model of pig liver esterase have been established as 6.2 x 3.1 x 4.7 Angstrom(3). It is believed that the current refinement completes the basic specification of the active site model and that, for the ma jority of practical applications of the enzyme, no significant further modifications are likely to be required.