Synthesis of a Biologically Active Nicotinic Acid Precursor: 2-Amino-3-hydroxybenzoic Acid

1948 ◽  
Vol 70 (5) ◽  
pp. 1847-1848 ◽  
Author(s):  
Joseph F. Nyc ◽  
Herschel K. Mitchell
Keyword(s):  
Nicotinic Acid ◽  
Biologically Active ◽  
Hydroxybenzoic Acid ◽  
Acid Precursor

The Nicotinic Acid-p-Aminophenylalanine-Hydroxybenzoic Acid Triads Induce Apoptosis in Human Leukemia U937 Cells

Heterocycles ◽  
2007 ◽  
Vol 71 (7) ◽  
pp. 1503 ◽  
Author(s):  
Akira Katoh ◽  
Mika Yamaguchi ◽  
Ryota Saito ◽  
Keiichiro Utsumi ◽  
Akira Ochiai ◽  
...  
Keyword(s):  
Nicotinic Acid ◽  
Hydroxybenzoic Acid ◽  
Human Leukemia ◽  
U937 Cells

A serum protease cleaves proANF into a 14-kilodalton peptide and ANF

1987 ◽  
Vol 252 (1) ◽  
pp. E147-E151
Author(s):  
K. D. Bloch ◽  
J. B. Zisfein ◽  
M. N. Margolies ◽  
C. J. Homcy ◽  
J. G. Seidman ◽  
...  
Keyword(s):  
Amino Acid ◽  
Culture Medium ◽  
Rat Plasma ◽  
Biologically Active ◽  
Amino Terminal ◽  
Isolation And Characterization ◽  
Amino Acid Precursor ◽  
Acid Precursor

Proatrial natriuretic factor (proANF), the 126-amino acid precursor of ANF, is the major storage form in mammalian atria. In contrast, two ANF peptides containing the 28- and 24-carboxyterminal residues of proANF have been isolated from rat plasma. Whether the cleavage of proANF in vivo to these ANF peptides occurs during or after its release into the circulation has not been determined. The latter possibility was suggested by our previous study where, by using a cultured rat cardiocyte preparation, we demonstrated that proANF is secreted intact into the culture medium. We now report that serum, but not plasma, contains a protease that specifically cleaves the 17-kdalton proANF to a 14-kdalton amino-terminal peptide and the carboxyterminal 3-kdalton circulating forms of ANF. The role of this proANF-cleaving enzyme in the generation of the biologically active ANF peptides remains to be defined. Its isolation and characterization should provide insights into its site of production and whether in vivo it is involved in the processing of circulating proANF.

scholarly journals Compounds from the Fruits of the Popular European Medicinal PlantVitex agnus-castusin Chemoprevention via NADP(H):Quinone Oxidoreductase Type 1 Induction

2013 ◽  
Vol 2013 ◽  
pp. 1-7 ◽  
Author(s):  
Shenghong Li ◽  
Shengxiang Qiu ◽  
Ping Yao ◽  
Handong Sun ◽  
Harry H. S. Fong ◽  
...  
Keyword(s):  
Biological Effects ◽  
Cancer Chemoprevention ◽  
2D Nmr ◽  
Biologically Active ◽  
Hydroxybenzoic Acid ◽  
Induction Effect ◽  
Quinone Oxidoreductase ◽  
Labdane Diterpene ◽  
First Time

As part of our continuing efforts in the search for potential biologically active compounds from medicinal plants, we have isolated 18 compounds including two novel nitrogen containing diterpenes from extracts of the fruits ofVitex agnus-castus. These isolates, along with our previously obtained novel compound vitexlactam A (1), were evaluated for potential biological effects, including cancer chemoprevention. Chemically, the nitrogenous isolates were found to be two labdane diterpene alkaloids, each containing anα,β-unsaturatedγ-lactam moiety. Structurally, they were elucidated to be 9α-hydroxy-13(14)-labden-16,15-amide (2) and 6β-acetoxy-9α-hydroxy-13(14)-labden-15,16-amide (3), which were named vitexlactams B and C, respectively. The 15 known isolates were identified as vitexilactone (4), rotundifuran (5), 8-epi-manoyl oxide (6), vitetrifolin D (7), spathulenol (8),cis-dihydro-dehydro-diconiferylalcohol-9-O-β-D-glucoside (9), luteolin-7-O-glucoside (10), 5-hydroxy-3,6,7,4′-tetramethoxyflavone (11), casticin (12), artemetin (13), aucubin (14), agnuside (15),β-sitosterol (16),p-hydroxybenzoic acid (17), andp-hydroxybenzoic acid glucose ester (18). All compound structures were determined/identified on the basis of 1D and/or 2D NMR and mass spectrometry techniques. Compounds6,8,9, and18were reported from aVitexspieces for the first time. The cancer chemopreventive potentials of these isolates were evaluated for NADP(H):quinone oxidoreductase type 1 (QR1) induction activity. Compound7demonstrated promising QR1 induction effect, while the new compound vitexlactam (3) was only slightly active.

scholarly journals Expanding the Myxochelin Natural Product Family by Nicotinic Acid Containing Congeners

2021 ◽  
Author(s):  
Nicolas A. Frank ◽  
Márió Széles ◽  
Sergi H. Akone ◽  
Sari Rasheed ◽  
Stephan Hüttel ◽  
...  
Keyword(s):  
Total Synthesis ◽  
Nicotinic Acid ◽  
Biosynthetic Pathway ◽  
Product Family ◽  
Biologically Active ◽  
Acid Moiety ◽  
Genome Data ◽  
Pure Compounds ◽  
Directed Biosynthesis ◽  
Improve Access

Myxobacteria represent a viable source of chemically diverse and biologically active secondary metabolites. The myxochelins are a well-studied family of catecholate-type siderophores produced by various myxobacterial strains. Here, we report the discovery, isolation and structure elucidation of three new myxochelins N1–N3 from the terrestrial myxobacterium Corallococcus sp. MCy9049, featuring an unusual nicotinic acid moiety. Precursor-directed biosynthesis (PDB) experiments and total synthesis were performed in order to confirm structures, improve access to pure compounds for bioactivity testing and to devise a biosynthesis proposal. The combined evaluation of metabolome and genome data covering myxobacteria supports the notion that the new myxochelin congeners reported here are in fact frequent side products of the known myxochelin A biosynthetic pathway in myxobacteria.

scholarly journals Expanding the Myxochelin Natural Product Family by Nicotinic Acid Containing Congeners

Molecules ◽  
2021 ◽  
Vol 26 (16) ◽  
pp. 4929
Author(s):  
Nicolas A. Frank ◽  
Márió Széles ◽  
Sergi H. Akone ◽  
Sari Rasheed ◽  
Stephan Hüttel ◽  
...  
Keyword(s):  
Total Synthesis ◽  
Nicotinic Acid ◽  
Biosynthetic Pathway ◽  
Product Family ◽  
Biologically Active ◽  
Acid Moiety ◽  
Genome Data ◽  
Pure Compounds ◽  
Directed Biosynthesis ◽  
Improve Access

Myxobacteria represent a viable source of chemically diverse and biologically active secondary metabolites. The myxochelins are a well-studied family of catecholate-type siderophores produced by various myxobacterial strains. Here, we report the discovery, isolation, and structure elucidation of three new myxochelins N1–N3 from the terrestrial myxobacterium Corallococcus sp. MCy9049, featuring an unusual nicotinic acid moiety. Precursor-directed biosynthesis (PDB) experiments and total synthesis were performed in order to confirm structures, improve access to pure compounds for bioactivity testing, and to devise a biosynthesis proposal. The combined evaluation of metabolome and genome data covering myxobacteria supports the notion that the new myxochelin congeners reported here are in fact frequent side products of the known myxochelin A biosynthetic pathway in myxobacteria.

The Pediocin AcH Precursor Is Biologically Active

1999 ◽  
Vol 65 (6) ◽  
pp. 2281-2286 ◽  
Author(s):  
Bibek Ray ◽  
Robin Schamber ◽  
Kurt W. Miller
Keyword(s):  
Amino Acid ◽  
Membrane Damage ◽  
Biologically Active ◽  
Leader Peptide ◽  
Chimeric Proteins ◽  
Cell Protection ◽  
E Coli ◽  
Amino Acid Precursor ◽  
Insight Into ◽  
Acid Precursor

ABSTRACT The properties of the pediocin AcH precursor, prepediocin AcH, have been studied to gain insight into how producer cells may protect themselves from the activity of intracellular prebacteriocins. The native 62-amino-acid precursor and the 44-amino-acid mature species were expressed in Escherichia coli host strains that lack the leader peptide processing enzyme, PapD. Both forms inhibited the growth of the test bacterium Listeria innocua Lin11, indicating that the native precursor is biologically active. The two species also were synthesized in the context of maltose-binding protein chimeric proteins to facilitate the measurement of their relative specific activities. The chimeric form of the precursor was ∼80% as active as the chimeric mature species. Of relevance to cell protection and pediocin AcH production, it was determined that the precursor is strongly susceptible to inactivation by reducing agents and to degradation by chymotrypsin and endogenous E. coliproteases. Taken together, the results indicate that the activity of prepediocin AcH may have to be controlled prior to secretion to prevent toxicity to the host. Perhaps producer cells avoid membrane damage by maintaining the precursor in a reduced inactive state or by degrading molecules whose secretion is delayed.

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