2-Amino-N-(2-furylmethyl)propanamide as a novel alanylglycine equivalent synthesized by bacilysin synthetase

Date

2003-10-08

Author

Tuzun, I
Karatas, AY
Sesenoglu, O
Demir, AS
Özcengiz, Gülay

Metadata

Show full item record

This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

Item Usage Stats

73
views

0
downloads

Bacilysin is a dipeptide antibiotic composed of L-alanine and L-anticapsin. We recently reported partial purification and characterization of the bacilysin synthetase. In the present study, L-anticapsin in the in vitro reaction mixture was replaced by furfurylamine, norephedrine, glycine, and benzylamine, respectively. The enzymatic biosynthesis of novel structures was checked by TLC analyses of reaction mixture extracts and any positive TLC result was verified by GC-MS analysis. The enzyme was shown to link furfurylamine to L-alanine, hence synthesizing 2-amino-N-(2-furylmethyl)propanamide, but did not act on the other substrates tested to replace anticapsin.

Subject Keywords

Biotechnology, Applied Microbiology and Biotechnology, Biochemistry

URI

https://hdl.handle.net/11511/43476

Journal

ENZYME AND MICROBIAL TECHNOLOGY

DOI

https://doi.org/10.1016/s0141-0229(03)00209-6

Collections

Department of Biology, Article

Suggestions

OpenMETU
Core

Bacilysin biosynthesis by a partially-purified enzyme fraction from Bacillus subtilis Yazgan, A; Özcengiz, Gülay; Ozcengiz, E; Kilinc, K; Marahiel, MA; Alaeddinoglu, NG (Elsevier BV, 2001-10-04) Biosynthesis of dipeptide antibiotic bacilysin by a partially purified enzyme prepared from Bacillus subtilis PY79 was studied. Cell material was desintegrated by treatment with lysozyme and sonication and the extract was subjected to ammonium sulfate fractionation. Bacilysin-synthesizing enzyme activity was precipitated between 40% to 70% ammonium sulfate saturation. In vitro enzymatical synthesis of bacilysin was confirmed by performing thin layer chromatographic comparison of the antibiotic formed with t...
Global Regulatory Systems Operating in Bacilysin Biosynthesis in Bacillus subtilis Koroglu, Turkan Ebru; Ogulur, Ismail; Mutlu, Seval; Karataş, Ayten; Özcengiz, Gülay (S. Karger AG, 2011-01-01) In Bacillus subtilis, bacilysin is a nonribosomally synthesized dipeptide antibiotic composed of L-alanine and L-anticapsin. The biosynthesis of bacilysin depends on the bacABCDEywfG operon (bac operon) and the adjacent ywfH gene. To elucidate the effects of global regulatory genes on the expression of bac operon, we used the combination of lacZ fusion analysis and the gel mobility shift assays. The cell density-dependent transition state induction of the bac operon was clearly shown. The basal expression l...
Analysis of a bac operon-silenced strain suggests pleiotropic effects of bacilysin in Bacillus subtilis Ertekin, Ozan; Taskin, Ash Aras; Demir, Mustafa; Karataş, Ayten; Özcengiz, Gülay (Springer Science and Business Media LLC, 2020-04-01) Bacilysin, as the simplest peptide antibiotic made up of only L-alanine and L-anticapsin, is produced and excreted by Bacillus subtilis under the control of quorum sensing. We analyzed bacilysin-nonproducing strain OGU1 which was obtained by bacA-targeted pMutin T3 insertion into the parental strain genome resulting in a genomic organization (bacA '::lacZ::erm::bacABCDEF) to form an IPTG-inducible bac operon. Although IPTG induction provided 3- to 5-fold increment in the transcription of bac operon genes, n...
Production, properties and application to biocatalysis of a novel extracellular alkaline phenol oxidase from the thermophilic fungus Scytalidium thermophilum Ögel, Zümrüt Begüm; Yuzugullu, Y.; Mete, S.; Bakir, U.; Kaptan, Y.; Sutay, D.; Demir, Ayhan Sıtkı (Springer Science and Business Media LLC, 2006-08-01) Scytalidium thermophilum produces an extracellular phenol oxidase on glucose-containing medium. Certain phenolic acids, specifically gallic acid and tannic acid, induce the expression of the enzyme. Production at 45 degrees C in batch cultures is growth-associated and is enhanced in the presence of 160 mu M CuSO4.5 H2O and 3 mM gallic acid. The highest enzyme activity is observed at pH 7.5 and 65 degrees C, on catechol. When incubated for 1 h at pH 7 and pH 8, 95% and 86% of the activity is retained. Thermo...
Killer toxin of Pichia anomala NCYC 432; purification, characterization and its exo-beta-1,3-glucanase activity Izgu, Fatih; Altinbay, Demet; Acun, Tolga (Elsevier BV, 2006-08-02) Pichia anomala NCYC 432 secretes a killer toxin which is inhibitory to a variety of yeasts including pathogenic Candida spp. The killer toxin in the culture supernatant was concentrated by ultratiltration and purified to homogenity by two successive gel filtration chromatographies with a TSK G2000SW column. Biochemical characterization of the toxin showed that it is a glycosylated protein with a molecular mass of 47 kDa and pI values of 3.4 and 3.7. The toxin showed high stability at pH values between 3 and...

Citation Formats

I. Tuzun, A. Karatas, O. Sesenoglu, A. Demir, and G. Özcengiz, “2-Amino-N-(2-furylmethyl)propanamide as a novel alanylglycine equivalent synthesized by bacilysin synthetase,” ENZYME AND MICROBIAL TECHNOLOGY, pp. 725–728, 2003, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/43476.