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@ARTICLE{Janowitz:31323,
author = {Janowitz, T. and Kneifel, H. and Piotrowski, M.},
title = {{I}dentification and characterization of plant agmatine
iminohydrolase, the last missing link in polyamine
biosynthesis of plants},
journal = {FEBS letters},
volume = {544},
issn = {0014-5793},
address = {Amsterdam [u.a.]},
publisher = {Elsevier},
reportid = {PreJuSER-31323},
pages = {258 - 261},
year = {2003},
note = {Record converted from VDB: 12.11.2012},
abstract = {The cloning, expression and characterization of plant
agmatine iminohydrolase (AIH, also known as agmatine
deiminase, EC 3.5.3.12) is described. Recombinant AIH of
Arabidopsis thaliana forms dimers and catalyzes the specific
conversion of agmatine to N-carbamoylputrescine and ammonia.
Biochemical data suggested that cysteine side chains are
involved in catalysis. However, site-directed mutagenesis of
the two highly conserved cysteine residues of AIH showed
that these cysteines are important but not essential for
activity, arguing against a thioester substrate-enzyme
intermediate during catalysis. This work represents the
completion of the cloning of the arginine decarboxylase
pathway genes of higher plants. (C) 2003 Published by
Elsevier Science B.V. on behalf of the Federation of
European Biochemical Societies.},
keywords = {J (WoSType)},
cin = {ICG-III},
ddc = {570},
cid = {I:(DE-Juel1)VDB49},
pnm = {Chemie und Dynamik der Geo-Biosphäre},
pid = {G:(DE-Juel1)FUEK257},
shelfmark = {Biochemistry $\&$ Molecular Biology / Biophysics / Cell
Biology},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000183393500048},
doi = {10.1016/S0014-5793(03)00515-5},
url = {https://juser.fz-juelich.de/record/31323},
}