Abstract
The study on the structural feature of carboxypeptidase A using transition state analog inhibitors suggests that the principal substrate recognition subsite of the enzyme is a pocket-shaped cavity having a rectangular opening with effective dimensions of 3.5 Å × 7.1 Å. The principal substrate recognition subsite (S1 ′ subsite) of Carboxypeptidase A is a pocket-shaped cavity having a rectangular opening with effective dimensions of 3.5 Å × 7.1 Å.
| Original language | English |
|---|---|
| Pages (from-to) | 317-322 |
| Number of pages | 6 |
| Journal | Bioorganic and Medicinal Chemistry Letters |
| Volume | 1 |
| Issue number | 6 |
| DOIs | |
| State | Published - 1991 |
Bibliographical note
Funding Information:AchowledgmenAt:u thors thank the Ministry of Education,R epublico f Korea for the financial supporto f this workt hrough the Basic ScienceI nstitute at POSTECH. Acknowledgemiesn ta lso duet o Prof. KwangS ooK im who provided molecular dimensions of naphthalenea nd helpful discussion.
Funding
AchowledgmenAt:u thors thank the Ministry of Education,R epublico f Korea for the financial supporto f this workt hrough the Basic ScienceI nstitute at POSTECH. Acknowledgemiesn ta lso duet o Prof. KwangS ooK im who provided molecular dimensions of naphthalenea nd helpful discussion.
| Funders |
|---|
| Ministry of Education,R epublico f Korea |
| Pohang University of Science and Technology |
ASJC Scopus subject areas
- Biochemistry
- Molecular Medicine
- Molecular Biology
- Pharmaceutical Science
- Drug Discovery
- Clinical Biochemistry
- Organic Chemistry