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Development of a Working Model of the Active Site in Bovine Lens Leucine Aminopeptidase: A Density Functional Investigation
Author(s) -
Erhardt Stefan,
Weston Jennie
Publication year - 2002
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20020104)3:1<101::aid-cbic101>3.0.co;2-2
Subject(s) - aminopeptidase , leucine , active site , lens (geology) , density functional theory , chemistry , crystal structure , enzyme , crystallography , biochemistry , amino acid , physics , optics , computational chemistry
The first coordination sphere geometry of a bimetallic enzyme , bovine lens leucine aminopeptidase, is reproduced in a model (shown in the picture) small enough for mechanistic studies of the active site to be carried out by using density functional theory. The minimalistic model is compared with the X‐ray crystal structure for the native enzyme.