التفاصيل البيبلوغرافية
العنوان: |
Dynamic properties of the first enzymatic reaction steps of porcine pancreatic elastase. How rigid is the active site of the native enzyme? Molecular dynamics simulation. |
المؤلفون: |
Geller M; Texas A&M University, Department of Biochemistry and Biophysics, College Station 77843., Carlson-Golab G, Lesyng B, Swanson SM, Meyer EF Jr |
المصدر: |
Biopolymers [Biopolymers] 1990; Vol. 30 (7-8), pp. 781-96. |
نوع المنشور: |
Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S. |
اللغة: |
English |
بيانات الدورية: |
Publisher: Wiley Country of Publication: United States NLM ID: 0372525 Publication Model: Print Cited Medium: Print ISSN: 0006-3525 (Print) Linking ISSN: 00063525 NLM ISO Abbreviation: Biopolymers Subsets: MEDLINE |
أسماء مطبوعة: |
Original Publication: New York, NY : Wiley |
مواضيع طبية MeSH: |
Pancreatic Elastase/*metabolism, Animals ; Binding Sites ; Computer Simulation ; Hydrogen Bonding ; Protein Conformation ; Swine |
مستخلص: |
Two molecular dynamics simulations (100 and 50 ps) of native porcine pancreatic elastase i.e., without bound substrate and with the active site hydrated by a dome of water (630 molecules) have been performed. Dynamical properties of the catalytic tetrad have been examined. While relative conformations of the Asp 102, His 57, and Ser 214 are rather stable in time, the side chain of Ser 195 undergoes several conformational changes. No preferences are observed for the formation of a hydrogen bond between the O gamma-H group (Ser 195) and nitrogen N, (His 57). A cluster of ordered water molecules effectively competes with the H-O gamma group (Ser 195) and thereby prevents the formation of this H bond, which is generally agreed to be crucial for catalysis. |
المشرفين على المادة: |
EC 3.4.21.36 (Pancreatic Elastase) |
تواريخ الأحداث: |
Date Created: 19900101 Date Completed: 19910301 Latest Revision: 20061115 |
رمز التحديث: |
20221208 |
DOI: |
10.1002/bip.360300713 |
PMID: |
2275978 |
قاعدة البيانات: |
MEDLINE |