Two phosphoenolpyruvate carboxykinases coexist in the Crassulacean Acid Metabolism plant Ananas comosus. Isolation and characterization of the smaller 65 kDa form

Copyright © 2011 Elsevier Masson SAS. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 49(2011), 6 vom: 01. Juni, Seite 646-53
1. Verfasser: Martín, Mariana (VerfasserIn)
Weitere Verfasser: Rius, Sebastián Pablo, Podestá, Florencio Esteban
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2011
Zugriff auf das übergeordnete Werk:Plant physiology and biochemistry : PPB
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Plant Proteins Protein Isoforms Oxaloacetic Acid 2F399MM81J Phosphoenolpyruvate 73-89-2 Phosphoenolpyruvate Carboxylase EC 4.1.1.31
LEADER 01000naa a22002652 4500
001 NLM206582021
003 DE-627
005 20231224000238.0
007 cr uuu---uuuuu
008 231224s2011 xx |||||o 00| ||eng c
024 7 |a 10.1016/j.plaphy.2011.02.015  |2 doi 
028 5 2 |a pubmed24n0689.xml 
035 |a (DE-627)NLM206582021 
035 |a (NLM)21398135 
040 |a DE-627  |b ger  |c DE-627  |e rakwb 
041 |a eng 
100 1 |a Martín, Mariana  |e verfasserin  |4 aut 
245 1 0 |a Two phosphoenolpyruvate carboxykinases coexist in the Crassulacean Acid Metabolism plant Ananas comosus. Isolation and characterization of the smaller 65 kDa form 
264 1 |c 2011 
336 |a Text  |b txt  |2 rdacontent 
337 |a ƒaComputermedien  |b c  |2 rdamedia 
338 |a ƒa Online-Ressource  |b cr  |2 rdacarrier 
500 |a Date Completed 06.12.2011 
500 |a Date Revised 30.09.2020 
500 |a published: Print-Electronic 
500 |a Citation Status MEDLINE 
520 |a Copyright © 2011 Elsevier Masson SAS. All rights reserved. 
520 |a Two phosphoenolpyruvate carboxykinase (PEPCK, EC 4.1.1.49) isoforms of 74 and 65 kDa were found to coexist in vivo in pineapple leaves, a constitutive Crassulacean Acid Metabolism plant. The 65 kDa form was not the result of proteolytic cleavage of the larger form since extraction methods reported to prevent PEPCK proteolysis in other plant tissues failed to yield a single immunoreactive PEPCK polypeptide in leaf extracts. In this work, the smaller form of 65 kDa was purified to homogeneity and physically and kinetically characterized and showed parameters compatible with a fully active enzyme. The specific activity was nearly twice higher for decarboxylation of oxaloacetate when compared to carboxylation of phosphoenolpyruvate. Kinetic parameters fell within the range of those estimated for other plant PEPCKs. Its activity was affected by several metabolites, as shown by inhibition by 3-phosphoglycerate, citrate, malate, fructose-1,6-bisphosphate, l-asparagine and activation of the decarboxylating activity by succinate. A break in the Arrhenius plot at about 30°C indicates that PEPCK structure is responsive to changes in temperature. The results indicate that pineapple leaves contain two PEPCK forms. The biochemical characterization of the smaller isoform performed in this work suggests that it could participate in both carbon and nitrogen metabolism in vivo by acting as a decarboxylase 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Protein Isoforms  |2 NLM 
650 7 |a Oxaloacetic Acid  |2 NLM 
650 7 |a 2F399MM81J  |2 NLM 
650 7 |a Phosphoenolpyruvate  |2 NLM 
650 7 |a 73-89-2  |2 NLM 
650 7 |a Phosphoenolpyruvate Carboxylase  |2 NLM 
650 7 |a EC 4.1.1.31  |2 NLM 
700 1 |a Rius, Sebastián Pablo  |e verfasserin  |4 aut 
700 1 |a Podestá, Florencio Esteban  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Plant physiology and biochemistry : PPB  |d 1991  |g 49(2011), 6 vom: 01. Juni, Seite 646-53  |w (DE-627)NLM098178261  |x 1873-2690  |7 nnns 
773 1 8 |g volume:49  |g year:2011  |g number:6  |g day:01  |g month:06  |g pages:646-53 
856 4 0 |u http://dx.doi.org/10.1016/j.plaphy.2011.02.015  |3 Volltext 
912 |a GBV_USEFLAG_A 
912 |a SYSFLAG_A 
912 |a GBV_NLM 
912 |a GBV_ILN_350 
951 |a AR 
952 |d 49  |j 2011  |e 6  |b 01  |c 06  |h 646-53