Unconventional serine proteases: Variations on the catalytic Ser/His/Asp triad configuration-Reference-Cited by-同舟云学术

Unconventional serine proteases: Variations on the catalytic Ser/His/Asp triad configuration

Published:2008-12 Issue:12 Volume:17 Page:2023-2037
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Ekici Özlem Doğan¹,Paetzel Mark²,Dalbey Ross E.¹

Affiliation:

1. Department of Chemistry, The Ohio State University, Columbus, Ohio 43210, USA

2. Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, V5A 1S6 Canada

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1110/ps.035436.108

Reference133 articles.

1. Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2·8 Å resolution

2. Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation

3. Handbook of proteolytic enzymes 2004 Elsevier London UK. N.N. Aronson A. Barret Glycosylasparaginase precursor and other self‐processing N‐terminal nucleophile amidohydrolases 2086 2089

4. Unusual 1H NMR chemical shifts support (His) Cepsilon 1---H{middle dot}{middle dot}{middle dot}O==C H-bond: Proposal for reaction-driven ring flip mechanism in serine protease catalysis

5. Confirmation of the assignment of the low-field proton resonance of serine proteases by using specifically nitrogen-15 labeled enzyme.

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