(Q27938241)

https://scigraph.springernature.com/pub.10.1007/s11745-008-3198-x

GOA release 2020-03-11

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1

Pruthvi Jayasimha

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author name string

W David Nes

series ordinal

2

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language of work or name

English

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publication date

August 2008

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1 December 2016

43

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issue

8

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page(s)

681-93

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exact match

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cites work

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Enzyme redesign and interactions of substrate analogues with sterol methyltransferase to understand phytosterol diversity, reaction mechanism and the nature of the active site

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Phytosterols, phytostanols, and their conjugates in foods: structural diversity, quantitative analysis, and health-promoting uses.

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Identification of the S-adenosyl-L-methionine binding site of protein-carboxyl O-methyltransferase using 8-azido-S-adenosyl-L-methionine.

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The Pneumocystis carinii drug target S-adenosyl-L-methionine:sterol C-24 methyl transferase has a unique substrate preference.

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Mechanistic analysis of a multiple product sterol methyltransferase implicated in ergosterol biosynthesis in Trypanosoma brucei

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Crystal structures of mycolic acid cyclopropane synthases from Mycobacterium tuberculosis

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New aspects of sterol biosynthesis in growth and development of higher plants.

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Site-Directed Mutagenesis of the Sterol Methyl Transferase Active Site from Saccharomyces cerevisiae Results in Formation of Novel 24-Ethyl Sterols

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Probing the sterol binding site of soybean sterol methyltransferase by site-directed mutagenesis: functional analysis of conserved aromatic amino acids in Region 1.

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Fatty acid and sterol metabolism: potential antimicrobial targets in apicomplexan and trypanosomatid parasitic protozoa

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Biosynthesis of phytosterols. Kinetic mechanism for the enzymatic C-methylation of sterols

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Many paths to methyltransfer: a chronicle of convergence

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Photoaffinity labeling of human placental NAD(+)-linked 15-hydroxyprostaglandin dehydrogenase with [alpha-32P]2N3NAD+. Identification of a peptide in the adenine ring binding domain

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Natural history of S-adenosylmethionine-binding proteins

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Molecular dissection of the S-adenosylmethionine-binding site of phosphatidylethanolamine N-methyltransferase

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Mapping and molecular modeling of S-adenosyl-L-methionine binding sites in N-methyltransferase domains of the multifunctional polypeptide cyclosporin synthetase.

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Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyltransferases, and suggests a catalytic mechanism for these enzymes.

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