An antibiotic (AH7) produced by Streptosporangium roseum strain 214 was investigated. This compound was extracted with chloroform from the filtrate culture and purified using thin-layer chromatography and high pressure liquid chromatography procedures. The antibiotic strongly inhibited the growth of several strains of fungi and bacteria known to be plant and human pathogens. This compound differed from all other antibiotics known to be synthesized by Streptosporangium spp. Some of its chemical and physical properties resembled those of maytansines produced by Nocardia but the antibiotic AH7 has only antibacterial and antitumoral activities.
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J Org Chem
August 2024
Center of Biosynthesis Technology, Asymchem Life Science (Tianjin) Co, Ltd, Tianjin 300457, P.R. China.
An enzyme catalyzed strategy for the synthesis of a chiral hydrazine from 3-cyclopentyl-3-oxopropanenitrile and hydrazine hydrate is presented. An imine reductase (IRED) from was identified to catalyze the reaction between 3-cyclopentyl-3-oxopropanenitrile and hydrazine hydrate to produce trace amounts of ()-3-cyclopentyl-3-hydrazineylpropanenitrile . We employed a 2-fold approach to optimize the catalytic performance of this enzyme.
View Article and Find Full Text PDFACS Synth Biol
February 2022
Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, People's Republic of China.
3-Hydroxy-l-tyrosine (l-DOPA) is a promising drug for treating Parkinson's disease. Tyrosine hydroxylase catalyzes the microbial synthesis of l-DOPA, which is hindered by the efficiency of catalysis, the supply of cofactor tetrahydrobiopterin, and the regulation of the pathway. In this study, the modular engineering strategy in was identified to effectively enhance l-DOPA production.
View Article and Find Full Text PDFAppl Microbiol Biotechnol
August 2020
Department of Biological Engineering, Utah State University, 4105 Old Main Hill, Logan, UT, 84322-4105, USA.
FR901533 (1, also known as WS79089B), WS79089A (2), and WS79089C (3) are polycyclic aromatic natural products with promising inhibitory activity to endothelin-converting enzymes. In this work, we isolated five tridecaketide products from Streptosporangium roseum No. 79089, including 1-3, benaphthamycin (4) and a novel FR901533 analogue (5).
View Article and Find Full Text PDFIUBMB Life
March 2019
Institute of Microbial Technology, Chandigarh, 160036, India.
The typical F-type lectin domain (FLD) has an L-fucose-binding motif [HX(26)RXDX(4)R/K] with conserved basic residues that mediate hydrogen bonding with alpha-L-fucose. About one-third of the nonredundant FLD sequences in the publicly available databases are "atypical"; they have motifs with substitutions of these critical residues and/or variations in motif length. We addressed the question if atypical FLDs with substitutions of the critical residues retain lectin activity by performing site-directed mutagenesis and assessing the glycan-binding functions of typical and atypical FLDs.
View Article and Find Full Text PDFGlycobiology
December 2018
Institute of Microbial Technology, Sector 39-A, Chandigarh, India.
Individual lectin-carbohydrate interactions are usually of low affinity. However, high avidity is frequently attained by the multivalent presentation of glycans on biological surfaces coupled with the occurrence of high order lectin oligomers or tandem repeats of lectin domains in the polypeptide. F-type lectins are l-fucose binding lectins with a typical sequence motif, HX(26)RXDX(4)R/K, whose residues participate in l-fucose binding.
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