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@ARTICLE{Janzik:9618,
author = {Janzik, I. and Macheroux, P. and Amrhein, N. and Schaller,
A.},
title = {{L}e{SBT}1, a subtilase from tomato plants},
journal = {The journal of biological chemistry},
volume = {275},
issn = {0021-9258},
address = {Bethesda, Md.},
publisher = {Soc.},
reportid = {PreJuSER-9618},
pages = {5193 - 5199},
year = {2000},
note = {Record converted from VDB: 12.11.2012},
abstract = {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.},
keywords = {J (WoSType)},
cin = {ICG-6},
ddc = {570},
cid = {I:(DE-Juel1)VDB144},
pnm = {Pflanzenphysiologie des Spurengasaustauschs mit der
Atmosphäre},
pid = {G:(DE-Juel1)FUEK82},
shelfmark = {Biochemistry $\&$ Molecular Biology},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000085378200092},
url = {https://juser.fz-juelich.de/record/9618},
}