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 40°C. 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 70°C. 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.
Кључне речи:
Leucine aminopeptidase / Low molecular weight autogenous inhibitor / Metalloenzyme / Monomeric / Streptomyces hygroscopicusИзвор:
Journal of Bioscience and Bioengineering, 2002, 94, 4, 309-314Издавач:
- Society of Fermentation and Bioengineering
DOI: 10.1016/S1389-1723(02)80169-4
ISSN: 1389-1723
WoS: 000180028800004
Scopus: 2-s2.0-0036429142
Институција/група
IHTMTY - JOUR AU - Karadžić, Ivanka AU - Izrael, Lidija AU - Gojgić-Cvijović, Gordana AU - Vujčić, Zoran PY - 2002 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/93 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 40°C. 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 70°C. 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 - Society of Fermentation and Bioengineering 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 and Izrael, Lidija and Gojgić-Cvijović, Gordana 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 40°C. 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 70°C. 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 = "Society of Fermentation and Bioengineering", 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., Izrael, L., Gojgić-Cvijović, G.,& Vujčić, Z.. (2002). Leucine aminopeptidase from Streptomyces hygroscopicus is controlled by a low molecular weight inhibitor. in Journal of Bioscience and Bioengineering Society of Fermentation and Bioengineering., 94(4), 309-314. https://doi.org/10.1016/S1389-1723(02)80169-4
Karadžić I, Izrael L, Gojgić-Cvijović G, 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, Izrael, Lidija, Gojgić-Cvijović, Gordana, 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 . .