• Journal of Microbiology and Biotechnology
• /
• v.11 no.6
• /
• pp.1011-1017
• /
• 2001

Streptomyces sp. Y-110 cytochrome P-450, induced by the addition of compactin -Na into the culture medium, was purified from the cell extract to apparent homogeniety, mainly by DEAE-Sepharose, hydroxyapatite, and Mono Q column chromatyography. The sepcific activity of purified enzyme on its substrate, compactin-Na, was determined to be 15 nmol of pravastatin per mg protein. The molecular mass of this enzyme on SDS-PAGE was $37{\pm}0.5$ kDa, pI was 4.5, and its CO difference spectrum showed maximum absorption peaks at 452 and 550nm, respectively. The N-terminal amino acid sequence was determined to be Met>Thr>Cys>Thr>Pro>Val>Thr>Val>The>Gly>Ala>Ala>Gly>Gln>Ile>Gly>Tyr>Ala>Leu. Its apparent $K_m$ on compactin-Na was $1.294{\mu}M{\cdot}min^-1,\;and\;V_{max}\;was\;1.028{\mu}M{\cdot}min^-1$. The maximum substrate concentration ($K_s$) for reaction was $270 {\mu}M$and thus $1/[K_s]$ was $3.7{\mu}M$. These physicochemical characteristics and kinetic behavior of this enzyme were compared and shown to be different from those of Streptomyces cytochrome P-450 enzymes reported, suggesting that this enzyme may be an additional member of the Streptomyces cytochrome P-450 family.

• Journal of Microbiology and Biotechnology
• /
• v.17 no.8
• /
• pp.1403-1406
• /
• 2007

An antiproliferative agent, streptochlorin, was isolated from the fermentation broth of a marine actinomycete isolated from marine sediment. Phylogenetic analysis of the 16S rRNA gene sequence indicated that the strain belongs to the genus Streptomyces. Bioactivity guided fractionation of the culture extract by solvent partitioning, ODS open flash chromatography, and reversed-phase HPLC gave a pure compound, streptochlorin. Its structure was elucidated by extensive 2D NMR and mass spectral analyses. Streptochlorin exhibited significant antiproliferative activity against human cultured cell lines.

• Proceedings of the Microbiological Society of Korea Conference
• /
• 2006.05a
• /
• pp.108-110
• /
• 2006

• Journal of Microbiology
• /
• v.34 no.2
• /
• pp.206-213
• /
• 1996

NADH-quinone reductase was purified 22-fold from the cytosolic fraction of Streptomyces sp. Imsnu-1 to apparent hemogenity, with an overall yield of 9%, by the purification procedure consisting of ammonium, sulfate precipitation and DEAE Sephacryl S-200 and DEAE 5 PW chromatographies. Thes molecular mass of the enzyme determined by gel filtration chromatography was found to be 110 kDa. SDS-PAGE revealed that the enzyme consists of two sugunits with a molecular mass of 54 kDa. The enzyme contained 1 mol of FMN per subunit as a cofactor. The $A_{272}$ A$_{457}$ ratio was 6.14 and the molar extinction coefficients were calculated to be 20, 800 and 25, 400M$^{-1}$ $cm^{-1}$ / AT 349 AND 457 nm, respectively. The N-terminal sequence of the enzyme contained the highly conserved fingerprint of ADP-binding domain. The enzyme used NADH as an electron donor and various quinones as electron acceptors. Cytochrome c was practically inactive. Air-stable flavin semiquinone was produced by the addition of NADH to the enzyme. Also, naphthosemiquinone was detected in the reaction mixture containing the enzyme.

• Applied Biological Chemistry
• /
• v.37 no.2
• /
• pp.110-114
• /
• 1994

In searching for new insecticidal compounds from soil microorganisms, strains of streptomyces species showed insecticidal activities on Musca domestica and Bombyx mori were selected. Compounds I-IV, which were isolated from the metabolites of no. 46 strain, were identified as piericidin $C_1$, $C_2$, $C_3$ and $D_1$, respectively by UV and NMR data analyses.

• Microbiology and Biotechnology Letters
• /
• v.30 no.2
• /
• pp.105-110
• /
• 2002

The sequence of 3,221 nucleotides immediately adjacent to rpsA gene encoding 30S ribosomal protein S1 of Brevibacterium ammoniagenes was determined. A putative open reading frame (ORF) of 2,670 nucleotides for a polypeptide of 889 amino acid residues and a TAG stop codon was found, which is located at a distance of 723 nucleotides upstream from rpsA gene with same translational direction. The deduced amino acid sequence of the ORF was found to be highly homologous to the DNA polymerase I of Streptomyces griseus (75.48％), Rhodococcus sp. ATCC 15963 (56.69％), Mycobacterium tuberculosis (55.46％) and Mycobacterium leprae (53.99％). It was suggested that the predicted product of the ORF is a DNA polymerase I with three functional domains. Two domains of 5 → 3 exonuclease and DNA polymerase are highly conserved with other DNA polymerase I, but 3 → 5 exonuclease domain is less conserved.