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Your search keyword '"Rebecca J M Goss"' showing total 3 results
Start Over Author "Rebecca J M Goss" Journal organic letters
3 results on '"Rebecca J M Goss"'

1. Zelkovamycins B–E, Cyclic Octapeptides Containing Rare Amino Acid Residues from an Endophytic Kitasatospora sp

Author

Xiaomeng Hao, Li-Yan Yu, Maoluo Gan, Rebecca J. M. Goss, Yufeng Liu, Shan Cen, Yujia Wang, Jack A. Connolly, Jiaqing Yu, and Yu-Qin Zhang

Subjects
010405 organic chemistry, Stereochemistry, Chemistry, Organic Chemistry, H1N1 influenza, 010402 general chemistry, Ring (chemistry), 01 natural sciences, Biochemistry, Virus, 0104 chemical sciences, Zelkovamycin, Kitasatospora sp, Gene cluster, Physical and Theoretical Chemistry, Amino acid residue
Abstract

Four unusual cyclopeptides, zelkovamycins B-E (1-4), were isolated from an endophytic Kitasatospora sp. Zelkovamycin B was featured by an unprecedented 3-methyl-5-hydroxypyrrolidine-2,4-dione ring system linked to the cyclopeptide skeleton. Their structures and full configurations were established by spectroscopic analysis, Marfey's method, and NMR calculations. A plausible biosynthetic pathway for zelkovamycins was proposed based on gene cluster analysis. Zelkovamycin E displayed potent inhibitory activity against H1N1 influenza A virus.

Published
2020
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2. Zelkovamycins B-E, Cyclic Octapeptides Containing Rare Amino Acid Residues from an Endophytic

Author

Xiaomeng, Hao, Jiaqing, Yu, Yujia, Wang, Jack A, Connolly, Yufeng, Liu, Yuqin, Zhang, Liyan, Yu, Shan, Cen, Rebecca J M, Goss, and Maoluo, Gan

Subjects
Influenza A Virus, H1N1 Subtype, Molecular Structure, Endophytes, Amino Acids, Peptides, Cyclic, Streptomyces, Antimicrobial Cationic Peptides
Abstract

Four unusual cyclopeptides, zelkovamycins B-E (

Published
2020

3. The first one-pot synthesis of L-7-iodotryptophan from 7-iodoindole and serine, and an improved synthesis of other L-7-halotryptophans

Author

Bert U. W. Maes, Wim Bert Griet Schepens, Rebecca J. M. Goss, Steven Ballet, Danai S. Gkotsi, Tom Willemse, and Duncan R. M. Smith

Subjects
Lysis, Indoles, biology, Molecular Structure, Chemistry, Organic Chemistry, One-pot synthesis, Tryptophan, Tryptophan synthase, Stereoisomerism, Biochemistry, Catalysis, Serine, Biotransformation, biology.protein, Tryptophan Synthase, Organic chemistry, Physical and Theoretical Chemistry, Hydrocarbons, Iodinated
Abstract

A simple and scalable one-pot biotransformation enables direct access to L-halotryptophans, including L-7-iodotryptophan, from the corresponding haloindoles. The biotransformation utilizes an easy to prepare bacterial cell lysate that may be stored as the lyophilizate for several months and utilized as a catalyst as and when required.

Published
2014

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