A glycolate dehydrogenase in the mitochondria of Arabidopsis thaliana

The fixation of molecular O2 by the oxygenase activity of Rubisco leads to the formation of phosphoglycolate in the chloroplast that is further metabolized in the process of photorespiration. The initial step of this pathway is the oxidation of glycolate to glyoxylate. Whereas in higher plants this...

Ausführliche Beschreibung

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 55(2004), 397 vom: 02. März, Seite 623-30
1. Verfasser: Bari, Rafijul (VerfasserIn)
Weitere Verfasser: Kebeish, Rashad, Kalamajka, Rainer, Rademacher, Thomas, Peterhänsel, Christoph
Format: Aufsatz
Sprache:English
Veröffentlicht: 2004
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Arabidopsis Proteins DNA Primers Glycolates Glyoxylates glycolic acid 0WT12SX38S Alcohol Oxidoreductases EC 1.1.- mehr... GDH protein, Arabidopsis EC 1.1.1.- glycollate oxidase EC 1.1.3.15 glyoxylic acid JQ39C92HH6
LEADER 01000naa a22002652 4500
001 NLM146696638
003 DE-627
005 20231223041741.0
007 tu
008 231223s2004 xx ||||| 00| ||eng c
028 5 2 |a pubmed24n0489.xml 
035 |a (DE-627)NLM146696638 
035 |a (NLM)14966218 
040 |a DE-627  |b ger  |c DE-627  |e rakwb 
041 |a eng 
100 1 |a Bari, Rafijul  |e verfasserin  |4 aut 
245 1 2 |a A glycolate dehydrogenase in the mitochondria of Arabidopsis thaliana 
264 1 |c 2004 
336 |a Text  |b txt  |2 rdacontent 
337 |a ohne Hilfsmittel zu benutzen  |b n  |2 rdamedia 
338 |a Band  |b nc  |2 rdacarrier 
500 |a Date Completed 19.07.2004 
500 |a Date Revised 24.11.2016 
500 |a published: Print-Electronic 
500 |a Citation Status MEDLINE 
520 |a The fixation of molecular O2 by the oxygenase activity of Rubisco leads to the formation of phosphoglycolate in the chloroplast that is further metabolized in the process of photorespiration. The initial step of this pathway is the oxidation of glycolate to glyoxylate. Whereas in higher plants this reaction takes place in peroxisomes and is dependent on oxygen as a co-factor, most algae oxidize glycolate in the mitochondria using organic co-factors. The identification and characterization of a novel glycolate dehydrogenase in Arabidopsis thaliana is reported here. The enzyme is dependent on organic co-factors and resembles algal glycolate dehydrogenases in its enzymatic properties. Mutants of E. coli incapable of glycolate oxidation can be complemented by overexpression of the Arabidopsis open reading frame. The corresponding RNA accumulates preferentially in illuminated leaves, but was also found in other tissues investigated. A fusion of the N-terminal part of the Arabidopsis glycolate dehydrogenase to red fluorescent protein accumulates in mitochondria when overexpressed in the homologous system. Based on these results it is proposed that the basic photorespiratory system of algae is conserved in higher plants 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Arabidopsis Proteins  |2 NLM 
650 7 |a DNA Primers  |2 NLM 
650 7 |a Glycolates  |2 NLM 
650 7 |a Glyoxylates  |2 NLM 
650 7 |a glycolic acid  |2 NLM 
650 7 |a 0WT12SX38S  |2 NLM 
650 7 |a Alcohol Oxidoreductases  |2 NLM 
650 7 |a EC 1.1.-  |2 NLM 
650 7 |a GDH protein, Arabidopsis  |2 NLM 
650 7 |a EC 1.1.1.-  |2 NLM 
650 7 |a glycollate oxidase  |2 NLM 
650 7 |a EC 1.1.3.15  |2 NLM 
650 7 |a glyoxylic acid  |2 NLM 
650 7 |a JQ39C92HH6  |2 NLM 
700 1 |a Kebeish, Rashad  |e verfasserin  |4 aut 
700 1 |a Kalamajka, Rainer  |e verfasserin  |4 aut 
700 1 |a Rademacher, Thomas  |e verfasserin  |4 aut 
700 1 |a Peterhänsel, Christoph  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Journal of experimental botany  |d 1985  |g 55(2004), 397 vom: 02. März, Seite 623-30  |w (DE-627)NLM098182706  |x 1460-2431  |7 nnns 
773 1 8 |g volume:55  |g year:2004  |g number:397  |g day:02  |g month:03  |g pages:623-30 
912 |a GBV_USEFLAG_A 
912 |a SYSFLAG_A 
912 |a GBV_NLM 
912 |a GBV_ILN_350 
951 |a AR 
952 |d 55  |j 2004  |e 397  |b 02  |c 03  |h 623-30