scholarly journals Characterization of SyrC, an Aminoacyltransferase Shuttling Threonyl and Chlorothreonyl Residues in the Syringomycin Biosynthetic Assembly Line

2007 ◽  
Vol 14 (1) ◽  
pp. 31-40 ◽  
Author(s):  
Gitanjali M. Singh ◽  
Frédéric H. Vaillancourt ◽  
Jun Yin ◽  
Christopher T. Walsh
Keyword(s):  
Assembly Line

Protein Assembly Line Components in Prodigiosin Biosynthesis:  Characterization of PigA,G,H,I,J

2006 ◽  
Vol 128 (39) ◽  
pp. 12600-12601 ◽  
Author(s):  
Sylvie Garneau-Tsodikova ◽  
Pieter C. Dorrestein ◽  
Neil L. Kelleher ◽  
Christopher T. Walsh
Keyword(s):  
Assembly Line ◽  
Protein Assembly

Characterization of the Post-Assembly Line Tailoring Processes in Teicoplanin Biosynthesis

2016 ◽  
Vol 11 (8) ◽  
pp. 2254-2264 ◽  
Author(s):  
Oleksandr Yushchuk ◽  
Bohdan Ostash ◽  
Thu H. Pham ◽  
Andriy Luzhetskyy ◽  
Victor Fedorenko ◽  
...  
Keyword(s):  
Assembly Line

Assembly-Line-Compatible Electromagnetic Characterization of Wearable Antenna Substrates

2017 ◽  
Vol 16 ◽  
pp. 1365-1368 ◽  
Author(s):  
Marco Rossi ◽  
Sam Agneessens ◽  
Hendrik Rogier ◽  
Dries Vande Ginste
Keyword(s):  
Assembly Line ◽  
Wearable Antenna

scholarly journals Thiocysteine lyases as polyketide synthase domains installing hydropersulfide into natural products and a hydropersulfide methyltransferase

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Song Meng ◽  
Andrew D. Steele ◽  
Wei Yan ◽  
Guohui Pan ◽  
Edward Kalkreuter ◽  
...  
Keyword(s):  
Natural Products ◽  
Natural Product ◽  
Assembly Line ◽  
Polyketide Synthase ◽  
Genome Mining ◽  
Assembly Lines ◽  
Biologically Relevant ◽  
Peptide Synthetase ◽  
Adenosyl Methionine

AbstractNature forms S-S bonds by oxidizing two sulfhydryl groups, and no enzyme installing an intact hydropersulfide (-SSH) group into a natural product has been identified to date. The leinamycin (LNM) family of natural products features intact S-S bonds, and previously we reported an SH domain (LnmJ-SH) within the LNM hybrid nonribosomal peptide synthetase (NRPS)-polyketide synthase (PKS) assembly line as a cysteine lyase that plays a role in sulfur incorporation. Here we report the characterization of an S-adenosyl methionine (SAM)-dependent hydropersulfide methyltransferase (GnmP) for guangnanmycin (GNM) biosynthesis, discovery of hydropersulfides as the nascent products of the GNM and LNM hybrid NRPS-PKS assembly lines, and revelation of three SH domains (GnmT-SH, LnmJ-SH, and WsmR-SH) within the GNM, LNM, and weishanmycin (WSM) hybrid NRPS-PKS assembly lines as thiocysteine lyases. Based on these findings, we propose a biosynthetic model for the LNM family of natural products, featuring thiocysteine lyases as PKS domains that directly install a -SSH group into the GNM, LNM, or WSM polyketide scaffold. Genome mining reveals that SH domains are widespread in Nature, extending beyond the LNM family of natural products. The SH domains could also be leveraged as biocatalysts to install an -SSH group into other biologically relevant scaffolds.

Biosynthesis of Himastatin: Assembly Line and Characterization of Three Cytochrome P450 Enzymes Involved in the Post-tailoring Oxidative Steps

2011 ◽  
Vol 123 (34) ◽  
pp. 7943-7948 ◽  
Author(s):  
Junying Ma ◽  
Zhongwen Wang ◽  
Hongbo Huang ◽  
Minghe Luo ◽  
Dianguang Zuo ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Assembly Line ◽  
Cytochrome P450 Enzymes

Biosynthesis of Himastatin: Assembly Line and Characterization of Three Cytochrome P450 Enzymes Involved in the Post-tailoring Oxidative Steps

2011 ◽  
Vol 50 (34) ◽  
pp. 7797-7802 ◽  
Author(s):  
Junying Ma ◽  
Zhongwen Wang ◽  
Hongbo Huang ◽  
Minghe Luo ◽  
Dianguang Zuo ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Assembly Line ◽  
Cytochrome P450 Enzymes

Morphological Characterization of Mycobacteriophage R1

1974 ◽  
Vol 32 ◽  
pp. 254-255
Author(s):  
B. L. Soloff ◽  
T. A. Rado
Keyword(s):  
Carbon Source ◽  
Stationary Phase ◽  
Growth Phase ◽  
Minimal Medium ◽  
Morphological Characterization ◽  
Logarithmic Growth Phase ◽  
Complete Lysis ◽  
Lysogenic Culture ◽  
Logarithmic Growth

Mycobacteriophage R1 was originally isolated from a lysogenic culture of M. butyricum. The virus was propagated on a leucine-requiring derivative of M. smegmatis, 607 leu−, isolated by nitrosoguanidine mutagenesis of typestrain ATCC 607. Growth was accomplished in a minimal medium containing glycerol and glucose as carbon source and enriched by the addition of 80 μg/ ml L-leucine. Bacteria in early logarithmic growth phase were infected with virus at a multiplicity of 5, and incubated with aeration for 8 hours. The partially lysed suspension was diluted 1:10 in growth medium and incubated for a further 8 hours. This permitted stationary phase cells to re-enter logarithmic growth and resulted in complete lysis of the culture.

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