Photoaffinity Labeling and Mutational Analysis of 24‐C‐Sterol Methyltransferase Defines the AdoMet Binding Site-Reference-Cited by-同舟云学术

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Photoaffinity Labeling and Mutational Analysis of 24‐C‐Sterol Methyltransferase Defines the AdoMet Binding Site

Published:2008-06-18 Issue:8 Volume:43 Page:681-693
ISSN:0024-4201
Container-title:Lipids
language:en
Short-container-title:Lipids

Author:

Jayasimha Pruthvi¹,Nes W. David¹

Affiliation:

1. Department of Chemistry and BiochemistryTexas Tech UniversityLubbockTX79409‐1061USA

Funder

National Science Foundation

Welch Foundation

Publisher

Wiley

Subject

Cell Biology,Organic Chemistry,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1007/s11745-008-3198-x

Reference38 articles.

1. STRUCTURE AND EVOLUTION OF ADOMET-DEPENDENT METHYLTRANSFERASES

2. Natural history of S-adenosylmethionine-binding proteins

3. Many paths to methyltransfer: a chronicle of convergence

4. Widespread Occurrence of Three Sequence Motifs in Diverse S-Adenosylmethionine-Dependent Methyltransferases Suggests a Common Structure for These Enzymes

5. Structure-guided Analysis Reveals Nine Sequence Motifs Conserved among DNA Amino-methyl-transferases, and Suggests a Catalytic Mechanism for these Enzymes

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4. A nematode sterol C4α-methyltransferase catalyzes a new methylation reaction responsible for sterol diversity;Journal of Lipid Research;2020-02

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