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4 results on '"Da-You Ma"'

1. Naturally-occurring spinosyn A and its derivatives function as argininosuccinate synthase activator and tumor inhibitor

Author

Zou Zizheng, Fan-Rong Kong, Chuanyu Yang, Chen Ling, Hu Xiyuan, Da-You Ma, Kun-Jian Peng, Xuan Li, Dong-Sheng Cao, Ceshi Chen, Tiao Luo, Zhengnan Ming, Wenjun Yi, Chen Xiaodan, Su-You Liu, Zhiyong Luo, Li Xia, Yuan-Zhu Xie, Jijia Li, Ousheng Liu, Junli Luo, Na Xu, Luo Wensong, and Min Wen

Subjects
0301 basic medicine, Argininosuccinate synthase, General Physics and Astronomy, Gene Knockout Techniques, Mice, chemistry.chemical_compound, 0302 clinical medicine, Citrulline, Breast, Natural products, Citrullinemia, Multidisciplinary, biology, Chemistry, Middle Aged, Cancer metabolism, Recombinant Proteins, Molecular Docking Simulation, Gene Knockdown Techniques, 030220 oncology & carcinogenesis, Pyrimidine metabolism, Female, Macrolides, Protein Binding, Adult, Urea cycle disorder, Science, Enzyme Activators, Breast Neoplasms, Argininosuccinate Synthase, Article, General Biochemistry, Genetics and Molecular Biology, 03 medical and health sciences, Target identification, Cell Line, Tumor, medicine, Animals, Humans, Metabolomics, Aged, Cell Proliferation, Aspartic Acid, Activator (genetics), Cell growth, Tumor Suppressor Proteins, General Chemistry, medicine.disease, Xenograft Model Antitumor Assays, HEK293 Cells, Pyrimidines, 030104 developmental biology, Mutation, Cancer cell, Cancer research, biology.protein
Abstract

Argininosuccinate synthase (ASS1) is a ubiquitous enzyme in mammals that catalyzes the formation of argininosuccinate from citrulline and aspartate. ASS1 genetic deficiency in patients leads to an autosomal recessive urea cycle disorder citrullinemia, while its somatic silence or down-regulation is very common in various human cancers. Here, we show that ASS1 functions as a tumor suppressor in breast cancer, and the pesticide spinosyn A (SPA) and its derivative LM-2I suppress breast tumor cell proliferation and growth by binding to and activating ASS1. The C13-C14 double bond in SPA and LM-2I while the Cys97 (C97) site in ASS1 are critical for the interaction between ASS1 and SPA or LM-2I. SPA and LM-2I treatment results in significant enhancement of ASS1 enzymatic activity in breast cancer cells, particularly in those cancer cells with low ASS1 expression, leading to reduced pyrimidine synthesis and consequently the inhibition of cancer cell proliferation. Thus, our results establish spinosyn A and its derivative LM-2I as potent ASS1 enzymatic activator and tumor inhibitor, which provides a therapeutic avenue for tumors with low ASS1 expression and for those non-tumor diseases caused by down-regulation of ASS1., Arginine addiction induced by argininosuccinate synthase (ASSN1) deficiency has been exploited to treat ASS1-deficient cancers. Here, the authors show an alternative therapeutic approach where ASS1 activity is increased by the pesticide spinosyn A and is shown to inhibit breast cancer cell proliferation.

Published
2021

2. Nitrile biotransformations for the synthesis of highly enantioenriched [beta]-hydroxy and [beta]-amino acid and amide derivatives: a general and simple but powerful and efficient benzyl protection strategy to increase enantioselectivity of the amidase

Author

Da-You Ma, De-Xian Wang, Jie Pan, Zhi-Tang Huang, and Mei-Xiang Wang

Subjects
Amino acids -- Chemical properties, Catalysis -- Analysis, Chirality -- Analysis, Nitriles -- Chemical properties, Biological sciences, Chemistry
Abstract

A Rhodococcus erythropolis AJ270, the nitrile hydratase and amidase-containing microbial whole cell catalyst, under very mild conditions were used to study the biotransformations of a number of racemic [beta]-hydroxy and [beta]-amino nitrile derivatives. The study provided an efficient and powerful approach to highly enantiopure [beta]-hydroxy and [beta]-amino acids and their amide derivatives that are valuable chiral intermediates in organic synthesis.

Published
2008

4. Nitrile Biotransformations for the Synthesis of Highly Enantioenriched β-Hydroxy and β-Amino Acid and Amide Derivatives: A General and Simple but Powerful and Efficient Benzyl Protection Strategy To Increase Enantioselectivity of the Amidase

Author

Da-You Ma, De-Xian Wang, Jie Pan, Zhi-Tang Huang, and Mei-Xiang Wang

Subjects
*BIOTRANSFORMATION (Metabolism), *NITRILES, *AMIDASES, *CATALYSTS, *ENANTIOSELECTIVE catalysis, *ACIDS, *AMIDES
Abstract

Biotransformations of a number of racemic β-hydroxy and β-amino nitrile derivatives were studied using Rhodococcus erythropolis AJ270, the nitrile hydratase and amidase-containing microbial whole cell catalyst, under very mild conditions. The overall enantioselectivity of nitrite biotransformations was governed predominantly by the amidase whose enantioselectivity was switched on remarkably by an O- and a N-benzyl protection group of the substrates. While biotransformations of β-hydroxy and β-amino alkanenitrites gave low yields of amide and acid products of very low enantiomeric purity, introduction of a simple benzyl protection group on the β-hydroxy and β-amino of nitrile substrates led to the formation of highly enantioenriched β-benzyloxy and β-benzylamino amides and acids in almost quantitative yield. The easy protection and deprotection operations, high chemical yield, and excellent enantioselectivity render the nitrite biotransformation a useful protocol in the synthesis of enantiopure β-hydroxy and β-amino acids. [ABSTRACT FROM AUTHOR]

Published
2008
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