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|a Biochemistry & Molecular Biology
100 1 _ |a Janzik, I.
|0 P:(DE-Juel1)129338
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|u FZJ
245 _ _ |a LeSBT1, a subtilase from tomato plants
260 _ _ |a Bethesda, Md.
|b Soc.
|c 2000
300 _ _ |a 5193 - 5199
336 7 _ |a Journal Article
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440 _ 0 |a Journal of Biological Chemistry
|x 0021-9258
|0 3091
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|v 275
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a The cDNA of a tomato subtilase designated LeSBT1 was cloned from a tomato flower cDNA library. The deduced amino acid sequence indicated for LeSBT1 the structure of a prepro-protein targeted to the secretory pathway by virtue of an amino-terminal signal peptide. LeSBT1 was expressed in the baculovirus/insect cell system and a processed 73-kDa form of LeSBT1, lacking both signal peptide and prodomain, was purified to homogeneity from culture supernatants, This 73-kDa LeSBT1, however, lacked proteolytic activity. Zymogen activation to yield 68-kDa LeSBT1 required the additional processing of an amino-terminal autoinhibitory peptide in a strictly pH-dependent manner. Mature 68-kDa LeSBT1 showed highest activity at acidic pH consistent with its presumed localization in the apoplast of the plant cell. In comparison to other plant subtilases, LeSBT1 exhibited a narrower substrate specificity in that it cleaves only polypeptide substrates preferentially but not exclusively carboxyl-terminal of glutamine residues. The possible involvement of LeSBT1 in selective proprotein processing is discussed with reference to the related mammalian proprotein convertases.
536 _ _ |a Pflanzenphysiologie des Spurengasaustauschs mit der Atmosphäre
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700 1 _ |a Macheroux, P.
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700 1 _ |a Amrhein, N.
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700 1 _ |a Schaller, A.
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773 _ _ |g Vol. 275, p. 5193 - 5199
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913 1 _ |k 36.61.0
|v Pflanzenphysiologie des Spurengasaustauschs mit der Atmosphäre
|l Umweltforschung
|b Umweltvorsorgeforschung
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914 1 _ |y 2000
915 _ _ |0 StatID:(DE-HGF)0010
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920 1 _ |k ICG-6
|l Biologie des Stoffaustauschs
|d 31.12.2001
|g ICG-6
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