Leucine aminopeptidase from Streptomyces hygroscopicus is controlled by a low molecular weight inhibitor
Само за регистроване кориснике
2002
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
In culture filtrate of Streptomyces hygroscopicus a producer of polyketide antibiotics, a leucine aminopeptidase and its autogenous inhibitor were detected. The leucine aminopeptidase was purified 4573-fold with yield of 82% by combination of ion exchange and hydrophobic chromatography. The enzyme is monomeric with a molecular mass of 51 kDa determined by gel chromatography and 67 kDa determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Optimal activity was at pH 8.0 and 40degreesC. The pI of leucine aminopeptidase is 8.2. The enzyme is strongly inhibited by 1,10-phenantroline, amastatin and dithiothreitol. Atomic absorption spectrometry indicated 2 mols of ion zinc per mol of enzyme. The enzyme is stable at up to 70degreesC. Leucine aminopeptidase prefers leucine and methionine as N-terminal amino acids. Activity of leucine aminopeptidase is strongly modulated by an autogenous low-molecular weight inhibitor during fermentation, especially during periods of intensiv...e antibiotic production.
Кључне речи:
Streptomyces hygroscopicus / leucine aminopeptidase / metalloenzyme / monomeric / low molecular weight autogenous inhibitorИзвор:
Journal of Bioscience and Bioengineering, 2002, 94, 4, 309-314Издавач:
- Soc Bioscience Bioengineering Japan, Osaka
DOI: 10.1016/S1389-1723(02)80169-4
ISSN: 1389-1723
PubMed: 16233308
WoS: 000180028800004
Scopus: 2-s2.0-0036429142
Колекције
Институција/група
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Karadžić, Ivanka M. AU - Izrael-Živković, Lidija AU - Gojgić-Cvijović, Gordana D. AU - Vujčić, Zoran PY - 2002 UR - https://cherry.chem.bg.ac.rs/handle/123456789/518 AB - In culture filtrate of Streptomyces hygroscopicus a producer of polyketide antibiotics, a leucine aminopeptidase and its autogenous inhibitor were detected. The leucine aminopeptidase was purified 4573-fold with yield of 82% by combination of ion exchange and hydrophobic chromatography. The enzyme is monomeric with a molecular mass of 51 kDa determined by gel chromatography and 67 kDa determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Optimal activity was at pH 8.0 and 40degreesC. The pI of leucine aminopeptidase is 8.2. The enzyme is strongly inhibited by 1,10-phenantroline, amastatin and dithiothreitol. Atomic absorption spectrometry indicated 2 mols of ion zinc per mol of enzyme. The enzyme is stable at up to 70degreesC. Leucine aminopeptidase prefers leucine and methionine as N-terminal amino acids. Activity of leucine aminopeptidase is strongly modulated by an autogenous low-molecular weight inhibitor during fermentation, especially during periods of intensive antibiotic production. PB - Soc Bioscience Bioengineering Japan, Osaka T2 - Journal of Bioscience and Bioengineering T1 - Leucine aminopeptidase from Streptomyces hygroscopicus is controlled by a low molecular weight inhibitor VL - 94 IS - 4 SP - 309 EP - 314 DO - 10.1016/S1389-1723(02)80169-4 ER -
@article{ author = "Karadžić, Ivanka M. and Izrael-Živković, Lidija and Gojgić-Cvijović, Gordana D. and Vujčić, Zoran", year = "2002", abstract = "In culture filtrate of Streptomyces hygroscopicus a producer of polyketide antibiotics, a leucine aminopeptidase and its autogenous inhibitor were detected. The leucine aminopeptidase was purified 4573-fold with yield of 82% by combination of ion exchange and hydrophobic chromatography. The enzyme is monomeric with a molecular mass of 51 kDa determined by gel chromatography and 67 kDa determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Optimal activity was at pH 8.0 and 40degreesC. The pI of leucine aminopeptidase is 8.2. The enzyme is strongly inhibited by 1,10-phenantroline, amastatin and dithiothreitol. Atomic absorption spectrometry indicated 2 mols of ion zinc per mol of enzyme. The enzyme is stable at up to 70degreesC. Leucine aminopeptidase prefers leucine and methionine as N-terminal amino acids. Activity of leucine aminopeptidase is strongly modulated by an autogenous low-molecular weight inhibitor during fermentation, especially during periods of intensive antibiotic production.", publisher = "Soc Bioscience Bioengineering Japan, Osaka", journal = "Journal of Bioscience and Bioengineering", title = "Leucine aminopeptidase from Streptomyces hygroscopicus is controlled by a low molecular weight inhibitor", volume = "94", number = "4", pages = "309-314", doi = "10.1016/S1389-1723(02)80169-4" }
Karadžić, I. M., Izrael-Živković, L., Gojgić-Cvijović, G. D.,& Vujčić, Z.. (2002). Leucine aminopeptidase from Streptomyces hygroscopicus is controlled by a low molecular weight inhibitor. in Journal of Bioscience and Bioengineering Soc Bioscience Bioengineering Japan, Osaka., 94(4), 309-314. https://doi.org/10.1016/S1389-1723(02)80169-4
Karadžić IM, Izrael-Živković L, Gojgić-Cvijović GD, Vujčić Z. Leucine aminopeptidase from Streptomyces hygroscopicus is controlled by a low molecular weight inhibitor. in Journal of Bioscience and Bioengineering. 2002;94(4):309-314. doi:10.1016/S1389-1723(02)80169-4 .
Karadžić, Ivanka M., Izrael-Živković, Lidija, Gojgić-Cvijović, Gordana D., Vujčić, Zoran, "Leucine aminopeptidase from Streptomyces hygroscopicus is controlled by a low molecular weight inhibitor" in Journal of Bioscience and Bioengineering, 94, no. 4 (2002):309-314, https://doi.org/10.1016/S1389-1723(02)80169-4 . .