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231224s2012 xx |||||o 00| ||eng c |
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|a 10.1016/j.plaphy.2012.02.006
|2 doi
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|a eng
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|a Gajda, Anna D
|e verfasserin
|4 aut
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|a Substrate specificity screening of oat (Avena sativa) seeds aminopeptidase demonstrate unusually broad tolerance in S1 pocket
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|c 2012
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|a ƒa Online-Ressource
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|a Date Completed 02.08.2012
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|a Date Revised 30.09.2020
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2012 Elsevier Masson SAS. All rights reserved.
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|a Aminopeptidases are proteolytic enzymes that remove one amino acid at a time from N-terminus of peptidic substrates. In plants, inhibitors of aminopeptidases can find potential applications in agriculture as herbicides. In this report we have used a library of fluorogenic derivatives of natural and unnatural amino acids for substrate specificity profiling of oat (Avena sativa) aminopeptidase. Interestingly, we have found that this enzyme recognizes effectively among the natural amino acids basic residues like Arg and Lys, hydrophobic Phe, Leu and Met, but also to some extent acidic residues Asp and Glu. In the case of unnatural amino acids hydrophobic residues (hPhe and hCha) and basic hArg were preferentially recognized
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Amino Acids
|2 NLM
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|a Aminopeptidases
|2 NLM
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|a EC 3.4.11.-
|2 NLM
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|a Pawełczak, Małgorzata
|e verfasserin
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|a Drag, Marcin
|e verfasserin
|4 aut
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|i Enthalten in
|t Plant physiology and biochemistry : PPB
|d 1991
|g 54(2012) vom: 30. Mai, Seite 6-9
|w (DE-627)NLM098178261
|x 1873-2690
|7 nnas
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|g volume:54
|g year:2012
|g day:30
|g month:05
|g pages:6-9
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|u http://dx.doi.org/10.1016/j.plaphy.2012.02.006
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