Using the Structure‐Function Linkage Database to Characterize Functional Domains in Enzymes-Reference-Cited by-同舟云学术

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Using the Structure‐Function Linkage Database to Characterize Functional Domains in Enzymes

Published:2014-12 Issue:1 Volume:48 Page:
ISSN:1934-3396
Container-title:Current Protocols in Bioinformatics
language:en
Short-container-title:Current Protocols in Bioinformatics

Author:

Brown Shoshana¹,Babbitt Patricia¹²³

Affiliation:

1. Department of Bioengineering and Therapeutic Sciences, University of California San Francisco California

2. Department of Pharmaceutical Chemistry, School of Pharmacy, University of California San Francisco California

3. California Institute for Quantitative Biosciences, University of California San Francisco California

Publisher

Wiley

Subject

General Medicine

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/0471250953.bi0210s48

Reference27 articles.

1. The Structure–Function Linkage Database

2. Understanding Enzyme Superfamilies

3. A Functionally Diverse Enzyme Superfamily that Abstracts the α Protons of Carboxylic Acids

4. Errors in genome annotation

5. D-galactonate utilisation by enteric bacteria The catabolic pathway inEscherichia coli

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1. Future Prospectives for Enzyme Technologies in the Food Industry;Enzymes in Food Biotechnology;2019

2. Deconvoluting the Reduction Potentials for the Three [4Fe-4S] Clusters in an AdoMet Radical SCIFF Maturase;Biochemistry;2018-10-01

3. Biochemical and Structural Characterization of a Schiff Base in the Radical-Mediated Biosynthesis of 4-Demethylwyosine by TYW1;Journal of the American Chemical Society;2018-05-24

4. 7-Carboxy-7-deazaguanine Synthase: A Radical S-Adenosyl-l-methionine Enzyme with Polar Tendencies;Journal of the American Chemical Society;2017-01-25

5. Biochemical and Spectroscopic Characterization of a Radical S-Adenosyl-l-methionine Enzyme Involved in the Formation of a Peptide Thioether Cross-Link;Biochemistry;2016-04-01

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