Escherichia coli Methionine Aminopeptidase: Implications of Crystallographic Analyses of the Native, Mutant, and Inhibited Enzymes for the Mechanism of Catalysis,-Reference-Cited by-同舟云学术

Escherichia coli Methionine Aminopeptidase: Implications of Crystallographic Analyses of the Native, Mutant, and Inhibited Enzymes for the Mechanism of Catalysis,

Published:1999-05-26 Issue:24 Volume:38 Page:7678-7688
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Lowther W. Todd¹,Orville Allen M.¹,Madden David T.¹,Lim Sejin¹,Rich Daniel H.¹,Matthews Brian W.¹

Affiliation:

1. Institute of Molecular Biology, Howard Hughes Medical Institute and Department of Physics, 1229 University of Oregon, Eugene, Oregon 97403, and Department of Chemistry and School of Pharmacy, University of WisconsinMadison, 425 North Charter Street, Madison Wisconsin 53706

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi990684r

Reference62 articles.

1. Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure

2. Crystal structure of methionine aminopeptidase from hyperthermophile, Pyrococcus furiosus a 1Edited by R. Huber

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