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20240114232503.0 |
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231223s2008 xx ||||| 00| ||eng c |
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|a pubmed24n1253.xml
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|a (DE-627)NLM174232713
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|a (NLM)17920159
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Ostrowski, Maciej
|e verfasserin
|4 aut
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|a Identification of enzyme activity that conjugates indole-3-acetic acid to aspartate in immature seeds of pea (Pisum sativum)
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|c 2008
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|a Text
|b txt
|2 rdacontent
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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| 338 |
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|a Band
|b nc
|2 rdacarrier
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| 500 |
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|a Date Completed 21.07.2008
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|a Date Revised 09.01.2024
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a This study describes the first identification of plant enzyme activity catalyzing the conjugation of indole-3-acetic acid to amino acids. Enzymatic synthesis of indole-3-acetylaspartate (IAA-Asp) by a crude enzyme preparation from immature seeds of pea (Pisum sativum) was observed. The reaction yielded a product with the same Rf as IAA-Asp standard after thin layer chromatography. The identity of IAA-Asp was verified by HPLC analysis. IAA-Asp formation was dependent on ATP and Mg2+, and was linear during a 60 min period. The enzyme preparation obtained after poly(ethylene glycol) 6000 fractionation showed optimum activity at pH 8.0, and the temperature optimum for IAA-Asp synthesis was 30 degrees C
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|a Journal Article
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| 650 |
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|a Research Support, Non-U.S. Gov't
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|a Indoleacetic Acids
|2 NLM
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| 650 |
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|a Plant Proteins
|2 NLM
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| 650 |
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|a Aspartic Acid
|2 NLM
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| 650 |
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7 |
|a 30KYC7MIAI
|2 NLM
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| 650 |
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|a indoleacetic acid
|2 NLM
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| 650 |
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|a 6U1S09C61L
|2 NLM
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| 650 |
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|a Ligases
|2 NLM
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| 650 |
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|a EC 6.-
|2 NLM
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| 700 |
1 |
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|a Jakubowska, Anna
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of plant physiology
|d 1979
|g 165(2008), 5 vom: 22., Seite 564-9
|w (DE-627)NLM098174622
|x 1618-1328
|7 nnns
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| 773 |
1 |
8 |
|g volume:165
|g year:2008
|g number:5
|g day:22
|g pages:564-9
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| 912 |
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|a GBV_USEFLAG_A
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|a SYSFLAG_A
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|a GBV_ILN_350
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| 951 |
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|a AR
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| 952 |
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|d 165
|j 2008
|e 5
|b 22
|h 564-9
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