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2. ChemInform Abstract: Quinoxapeptins: Novel Chromodepsipeptide Inhibitors of HIV-1 and HIV-2 Reverse Transcriptase. Part 1. The Producing Organism and Biological Activity.

Author

LINGHAM, R. B., primary, HSU, A. H. M., additional, O'BRIEN, J. A., additional, SIGMUND, J. M., additional, SANCHEZ, M., additional, GAGLIARDI, M. M., additional, HEIMBUCH, B. K., additional, GENILLOUD, O., additional, MARTIN, I., additional, DIEZ, M. T., additional, HIRSCH, C. F., additional, ZINK, D. L., additional, LIESCH, J. M., additional, KOCH, G. E., additional, GARTNER, S. E., additional, GARRITY, G. M., additional, TSOU, N. N., additional, and SALITURO, G. M., additional

Published
2010
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4. Quinoxapeptins: novel chromodepsipeptide inhibitors of HIV-1 and HIV-2 reverse transcriptase. I. The producing organism and biological activity.

Author

Lingham RB, Hsu AH, O'Brien JA, Sigmund JM, Sanchez M, Gagliardi MM, Heimbuch BK, Genilloud O, Martin I, Diez MT, Hirsch CF, Zink DL, Liesch JM, Koch GE, Gartner SE, Garrity GM, Tsou NN, and Salituro GM

Subjects
Actinomycetales classification, Actinomycetales metabolism, HIV Reverse Transcriptase, HIV-1 genetics, Humans, Hydroxyquinolines chemistry, Hydroxyquinolines pharmacology, In Vitro Techniques, Kinetics, Molecular Structure, Mutation, Nucleic Acid Synthesis Inhibitors, Peptides, Cyclic chemistry, Quinoxalines chemistry, RNA-Directed DNA Polymerase genetics, Reverse Transcriptase Inhibitors chemistry, HIV-1 enzymology, HIV-2 enzymology, Peptides, Cyclic metabolism, Peptides, Cyclic pharmacology, Quinoxalines metabolism, Quinoxalines pharmacology, RNA-Directed DNA Polymerase metabolism, Reverse Transcriptase Inhibitors metabolism, Reverse Transcriptase Inhibitors pharmacology
Abstract

Quinoxapeptin A and B are novel chromodepsipeptides which were isolated from a nocardioform actinomycete with indeterminant morphology. Quinoxapeptins A and B are potent inhibitors of HIV-1 and HIV-2 reverse transcriptase and almost equally active against two single mutants forms as well as a double mutant form of HIV-1 reverse transcriptase. Quinoxapeptin A and B are specific inhibitors of HIV-1 and HIV-2 reverse transcriptase because they did not inhibit human DNA polymerase alpha, beta, gamma and delta. Quinoxapeptin A and B are structurally similar to luzopeptin A which was also active against HIV-1 and HIV-2 reverse transcriptase.

Published
1996
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5. Chaetomella acutiseta produces chaetomellic acids A and B which are reversible inhibitors of farnesyl-protein transferase.

Author

Lingham RB, Silverman KC, Bills GF, Cascales C, Sanchez M, Jenkins RG, Gartner SE, Martin I, Diez MT, and Peláez F

Subjects
Fermentation, Maleates isolation & purification, Maleates pharmacology, Alkyl and Aryl Transferases, Maleates metabolism, Mitosporic Fungi metabolism, Transferases antagonists & inhibitors
Abstract

Chaetomellic acids A and B, isolated from Chaetomella acutiseta, are specific inhibitors of farnesyl-protein transferase that do not inhibit geranylgeranyl transferase type 1 or squalene synthase. Chaetomellic acids A and B are reversible inhibitors, resemble farnesyl diphosphate and probably inhibit FPTase by substituting for farnesyl diphosphate. Chaetomellic acid production appears to be widespread within the genus Chaetomella.

Published
1993
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