Metal- and Serine-Dependent Meta-Cleavage Product Hydrolases Utilize Similar Nucleophile-Activation Strategies-Reference-Cited by-同舟云学术

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Metal- and Serine-Dependent Meta-Cleavage Product Hydrolases Utilize Similar Nucleophile-Activation Strategies

Published:2018-10-30 Issue:12 Volume:8 Page:11622-11632
ISSN:2155-5435
Container-title:ACS Catalysis
language:en
Short-container-title:ACS Catal.

Author:

Kuatsjah Eugene,Chan Anson C. K.,Hurst Timothy E.¹,Snieckus Victor¹,Murphy Michael E. P.^ORCID,Eltis Lindsay D.^ORCID

Affiliation:

1. Department of Chemistry, Queen’s University, Kingston, Ontario, Canada K7L 3N6

Funder

Biological and Environmental Research

Canada Research Chairs

Natural Sciences and Engineering Research Council of Canada

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Catalysis,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acscatal.8b02955

Reference35 articles.

1. Emergent mechanistic diversity of enzyme-catalysed β-diketone cleavage

2. Mechanistic Inferences from the Crystal Structure of Fumarylacetoacetate Hydrolase with a Bound Phosphorus-based Inhibitor

3. IpdAB, a virulence factor in Mycobacterium tuberculosis, is a cholesterol ring-cleaving hydrolase

4. Identification of an Acyl-Enzyme Intermediate in a meta-Cleavage Product Hydrolase Reveals the Versatility of the Catalytic Triad

5. The α/β-Hydrolase Fold 3DM Database (ABHDB) as a Tool for Protein Engineering

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4. Artificial phosphatase upon premicellar nanoarchitectonics of lanthanum complexes with long-chained imidazole derivatives;Journal of Colloid and Interface Science;2022-12

5. How to complete the tautomerization and substrate-assisted activation prior to C–C bond fission by meta-cleavage product hydrolase LigY?;Catalysis Science & Technology;2020

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