Characterization of the promiscuous N-acyl CoA transferase, LgoC, in legonoxamine biosynthesis

2020 ◽  
Vol 18 (12) ◽  
pp. 2219-2222 ◽  
Author(s):  
Fleurdeliz Maglangit ◽  
Saad Alrashdi ◽  
Justine Renault ◽  
Laurent Trembleau ◽  
Catherine Victoria ◽  
...  
Keyword(s):  
Micrococcus Luteus ◽  
Coa Transferase ◽  
Hydroxamate Siderophores

More than 500 siderophores are known to date, but only three were identified to be aryl-containing hydroxamate siderophores, legonoxamines A and B from Streptomyces sp. MA37, and aryl ferrioxamine 2 from Micrococcus luteus KLE1011.

scholarly journals Isolation and Characterization of Antibacterial Carotane Sesquiterpenes from Artemisia argyi Associated Endophytic Trichoderma virens QA-8

Antibiotics ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 213
Author(s):  
Xiao-Shan Shi ◽  
Yin-Ping Song ◽  
Ling-Hong Meng ◽  
Sui-Qun Yang ◽  
Dun-Jia Wang ◽  
...  
Keyword(s):  
Endophytic Fungus ◽  
Micrococcus Luteus ◽  
Crystallographic Analysis ◽  
Medicinal Herb ◽  
Trichoderma Virens ◽  
Isolation And Characterization ◽  
Artemisia Argyi ◽  
Detailed Interpretation ◽  
Fungal Kingdom

Carotane sesquiterpenes are commonly found in plants but are infrequently reported in the fungal kingdom. Chemical investigation of Trichoderma virens QA-8, an endophytic fungus associated with the inner root tissue of the grown medicinal herb Artemisia argyi H. Lév. and Vaniot, resulted in the isolation and characterization of five new carotane sesquiterpenes trichocarotins I–M (1–5), which have diverse substitution patterns, and seven known related analogues (6–12). The structures of these compounds were established on the basis of a detailed interpretation of their NMR and mass spectroscopic data, and the structures including the relative and absolute configurations of compounds 1–3, 5, 9, and 10 were confirmed by X-ray crystallographic analysis. In the antibacterial assays, all isolates exhibited potent activity against Escherichia coli EMBLC-1, with MIC values ranging from 0.5 to 32 µg/mL, while 7β-hydroxy CAF-603 (7) strongly inhibited Micrococcus luteus QDIO-3 (MIC = 0.5 µg/mL). Structure-activity relationships of these compounds were discussed. The results from this study demonstrate that the endophytic fungus T. virens QA-8 from the planted medicinal herb A. argyi is a rich source of antibacterial carotane sesquiterpenes, and some of them might be interesting for further study to be developed as novel antibacterial agents.

Characterization of propionate CoA-transferase from Ralstonia eutropha H16

2013 ◽  
Vol 98 (8) ◽  
pp. 3579-3589 ◽  
Author(s):  
Elena Volodina ◽  
Marc Schürmann ◽  
Nicole Lindenkamp ◽  
Alexander Steinbüchel
Keyword(s):  
Ralstonia Eutropha ◽  
Coa Transferase ◽  
Ralstonia Eutropha H16

Discovery and Characterization of New Hydroxamate Siderophores, Baumannoferrin A and B, produced byAcinetobacter baumannii

ChemBioChem ◽  
2015 ◽  
Vol 16 (13) ◽  
pp. 1896-1904 ◽  
Author(s):  
William F. Penwell ◽  
Nancy DeGrace ◽  
Sharon Tentarelli ◽  
Lise Gauthier ◽  
Catherine M. Gilbert ◽  
...  
Keyword(s):  
Hydroxamate Siderophores

Purification and Characterization of a Unique Alkaline Elastase from Micrococcus luteus

2000 ◽  
Vol 18 (1) ◽  
pp. 46-55 ◽  
Author(s):  
Deborah J Clark ◽  
Steven J Hawrylik ◽  
Edward Kavanagh ◽  
Dennis J Opheim
Keyword(s):  
Micrococcus Luteus ◽  
Purification And Characterization

scholarly journals Degradation of Aromatics and Chloroaromatics by Pseudomonas sp. Strain B13: Cloning, Characterization, and Analysis of Sequences Encoding 3-Oxoadipate:Succinyl-Coenzyme A (CoA) Transferase and 3-Oxoadipyl-CoA Thiolase

2002 ◽  
Vol 184 (1) ◽  
pp. 216-223 ◽  
Author(s):  
Markus Göbel ◽  
Kerstin Kassel-Cati ◽  
Eberhard Schmidt ◽  
Walter Reineke
Keyword(s):  
Amino Acids ◽  
Coenzyme A ◽  
Tricarboxylic Acid Cycle ◽  
Tricarboxylic Acid ◽  
Open Reading Frames ◽  
Amino Acid Residues ◽  
Coa Transferase ◽  
Tricarboxylic Acid Cycle Intermediates ◽  
Reading Frames

ABSTRACT 3-Oxoadipate:succinyl-coenzyme A (CoA) transferase and 3-oxoadipyl-CoA thiolase carry out the ultimate steps in the conversion of benzoate and 3-chlorobenzoate to tricarboxylic acid cycle intermediates in bacteria utilizing the 3-oxoadipate pathway. This report describes the characterization of DNA fragments with the overall length of 5.9 kb from Pseudomonas sp. strain B13 that encode these enzymes. DNA sequence analysis revealed five open reading frames (ORFs) plus an incomplete one. ORF1, of unknown function, has a length of 414 bp. ORF2 (catI) encodes a polypeptide of 282 amino acids and starts at nucleotide 813. ORF3 (catJ) encodes a polypeptide of 260 amino acids and begins at nucleotide 1661. CatI and CatJ are the subunits of the 3-oxoadipate:succinyl-CoA transferase, whose activity was demonstrated when both genes were ligated into expression vector pET11a. ORF4, termed catF, codes for a protein of 401 amino acid residues with a predicted mass of 41,678 Da with 3-oxoadipyl-CoA thiolase activity. The last three ORFs seem to form an operon since they are oriented in the same direction and showed an overlapping of 1 bp between catI and catJ and of 4 bp between catJ and catF. Conserved functional groups important for the catalytic activity of CoA transferases and thiolases were identified in CatI, CatJ, and CatF. ORF5 (catD) encodes the 3-oxoadipate enol-lactone hydrolase. An incomplete ORF6 of 1,183 bp downstream of ORF5 and oriented in the opposite direction was found. The protein sequence deduced from ORF6 showed a putative AMP-binding domain signature.

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