Mg-dechelation activity in radish cotyledons with artificial and native substrates, Mg-chlorophyllin a and chlorophyllide a

The Mg-dechelation activity in extracts from radish (Raphanus sativus L.) cotyledons was investigated using an artificial substrate, Mg-chlorophyllin a (Chlin) and the native substrate, chlorophyllide a (Chlide). In addition to a known a small molecular weight metal-chelating substance (MCS), Mg-rel...

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Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 43(2005), 5 vom: 01. Mai, Seite 459-64
1. Verfasser: Suzuki, Toshiyuki (VerfasserIn)
Weitere Verfasser: Kunieda, Tadashi, Murai, Fumiko, Morioka, Satoshi, Shioi, Yuzo
Format: Aufsatz
Sprache:English
Veröffentlicht: 2005
Zugriff auf das übergeordnete Werk:Plant physiology and biochemistry : PPB
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Chelating Agents Chlorophyllides Enzyme Inhibitors Enzymes magnesium dechelatase chlorophyllide a 14897-06-4 Azetidinecarboxylic Acid mehr... 5GZ3E0L9ZU Edetic Acid 9G34HU7RV0 Metalloendopeptidases EC 3.4.24.- chlorophyllin EEM82VOY7C mugineic acid KR256JY76I
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100 1 |a Suzuki, Toshiyuki  |e verfasserin  |4 aut 
245 1 0 |a Mg-dechelation activity in radish cotyledons with artificial and native substrates, Mg-chlorophyllin a and chlorophyllide a 
264 1 |c 2005 
336 |a Text  |b txt  |2 rdacontent 
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500 |a Date Completed 27.10.2005 
500 |a Date Revised 30.09.2020 
500 |a published: Print-Electronic 
500 |a Citation Status MEDLINE 
520 |a The Mg-dechelation activity in extracts from radish (Raphanus sativus L.) cotyledons was investigated using an artificial substrate, Mg-chlorophyllin a (Chlin) and the native substrate, chlorophyllide a (Chlide). In addition to a known a small molecular weight metal-chelating substance (MCS), Mg-releasing protein (MRP) was present when Chlin was used as the substrate. However, only MCS had Mg-dechelation activity with the native substrate. To examine the possibility of the dissociation of MRP into a protein moiety and a small molecular mass compound with an activity like MCS, extraction with low and high ionic strength buffers was carried out. No evidence was obtained that MCS is a moiety of MRP, however. Inhibitor studies showed that MCS and MRP had different susceptibilities to the inhibitors, especially to the chelators tiron and EDTA when Chlin was used as the substrate. Tiron had no effect on MRP, but it severely reduced MCS activity in both substrates. The activity of MRP increased during senescence, indicating the induction of MRP, while the activity of MCS was almost unchanged. These results suggest different reaction mechanisms by independent compounds. These findings suggest that MRP and MCS are present independently, and MCS is postulated to be a substance that catalyzes the Mg-dechelation reaction in the breakdown pathway of Chl, although MCS was not induced during senescence. The properties of MRP and MCS in relation to the small molecular mass substance obtained from strawberry fruit are also discussed 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
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650 7 |a Chlorophyllides  |2 NLM 
650 7 |a Enzyme Inhibitors  |2 NLM 
650 7 |a Enzymes  |2 NLM 
650 7 |a magnesium dechelatase  |2 NLM 
650 7 |a chlorophyllide a  |2 NLM 
650 7 |a 14897-06-4  |2 NLM 
650 7 |a Azetidinecarboxylic Acid  |2 NLM 
650 7 |a 5GZ3E0L9ZU  |2 NLM 
650 7 |a Edetic Acid  |2 NLM 
650 7 |a 9G34HU7RV0  |2 NLM 
650 7 |a Metalloendopeptidases  |2 NLM 
650 7 |a EC 3.4.24.-  |2 NLM 
650 7 |a chlorophyllin  |2 NLM 
650 7 |a EEM82VOY7C  |2 NLM 
650 7 |a mugineic acid  |2 NLM 
650 7 |a KR256JY76I  |2 NLM 
700 1 |a Kunieda, Tadashi  |e verfasserin  |4 aut 
700 1 |a Murai, Fumiko  |e verfasserin  |4 aut 
700 1 |a Morioka, Satoshi  |e verfasserin  |4 aut 
700 1 |a Shioi, Yuzo  |e verfasserin  |4 aut 
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