Zinc Coordination Geometry and Ligand Binding Affinity: The Structural and Kinetic Analysis of the Second-Shell Serine 228 Residue and the Methionine 180 Residue of the Aminopeptidase from Vibrio proteolyticus-Reference-Cited by-同舟云学术

Zinc Coordination Geometry and Ligand Binding Affinity: The Structural and Kinetic Analysis of the Second-Shell Serine 228 Residue and the Methionine 180 Residue of the Aminopeptidase from Vibrio proteolyticus

Published:2008-06-25 Issue:29 Volume:47 Page:7673-7683
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Ataie Niloufar J.¹,Hoang Quyen Q.¹,Zahniser Megan P. D.¹,Tu Yupeng¹,Milne Amy¹,Petsko Gregory A.¹,Ringe Dagmar¹

Affiliation:

1. Rosenstiel Basic Medical Sciences Research Center and Departments of Biochemistry and Chemistry, Program in Biochemistry and Biophysics, Brandeis University, 415 South Street, Waltham, Massachusetts 02454

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi702188e

Reference50 articles.

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4. Metalloenzymes: the entatic nature of their active sites.

5. Energised (entatic) States of Groups and of Secondary Structures in Proteins and Metalloproteins

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