d-GLYCERATE 3-KINASE, the Last Unknown Enzyme in the Photorespiratory Cycle in Arabidopsis, Belongs to a Novel Kinase Family

Boldt, Ralf; Edner, Christoph; Kolukisaoglu, Üner; Hagemann, Martin; Weckwerth, Wolfram; Wienkoop, Stefanie; Morgenthal, Katja; Bauwe, Hermann

doi:10.1105/tpc.105.033993

Cited by 137 publications

(132 citation statements)

References 43 publications

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“…Parts of the PCOC (glycerate dehydrogenase, serine transminases and serine hydroxymethyltransferase) could have been recruited from core metabolism synthesizing serine and glycine from glycolytic intermediates, while others (glycolate dehydrogenase/oxidase, glycine decarboxylase and glycerate kinase) have no known roles other than in the metabolism of glycolate to PCRC intermediates [93,94].…”

Section: Oxygen Accumulation Rubisco Oxygenase and The Metabolism Ofmentioning

confidence: 99%

Algal evolution in relation to atmospheric CO ₂ : carboxylases, carbon-concentrating mechanisms and carbon oxidation cycles

Raven

Giordano

Beardall

et al. 2012

Phil. Trans. R. Soc. B

251

209

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Oxygenic photosynthesis evolved at least 2.4 Ga; all oxygenic organisms use the ribulose bisphosphate carboxylase-oxygenase (Rubisco) -photosynthetic carbon reduction cycle (PCRC) rather than one of the five other known pathways of autotrophic CO 2 assimilation. The high CO 2 and (initially) O 2 -free conditions permitted the use of a Rubisco with a high maximum specific reaction rate. As CO 2 decreased and O 2 increased, Rubisco oxygenase activity increased and 2-phosphoglycolate was produced, with the evolution of pathways recycling this inhibitory product to sugar phosphates. Changed atmospheric composition also selected for Rubiscos with higher CO 2 affinity and CO 2 /O 2 selectivity correlated with decreased CO 2 -saturated catalytic capacity and/or for CO 2 -concentrating mechanisms (CCMs). These changes increase the energy, nitrogen, phosphorus, iron, zinc and manganese cost of producing and operating Rubisco -PCRC, while biosphere oxygenation decreased the availability of nitrogen, phosphorus and iron. The majority of algae today have CCMs; the timing of their origins is unclear. If CCMs evolved in a low-CO 2 episode followed by one or more lengthy high-CO 2 episodes, CCM retention could involve a combination of environmental factors known to favour CCM retention in extant organisms that also occur in a warmer high-CO 2 ocean. More investigations, including studies of genetic adaptation, are needed.

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Section: Oxygen Accumulation Rubisco Oxygenase and The Metabolism Ofmentioning

confidence: 99%

Algal evolution in relation to atmospheric CO ₂ : carboxylases, carbon-concentrating mechanisms and carbon oxidation cycles

Raven

Giordano

Beardall

et al. 2012

Phil. Trans. R. Soc. B

251

209

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“…Hence, we used the Arabidopsis (Arabidopsis thaliana) GLYK sequence (Boldt et al, 2005) for similarity searches in maize EST libraries and identified several overlapping ESTs, which were combined to a continuous nucleotide sequence encoding the full-length putative ZmGLYK. This sequence was recently deposited in GenBank, and the gene product was tentatively annotated as hypothetical protein LOC100274052 (Alexandrov et al, 2009).…”

Section: Resultsmentioning

confidence: 99%

“…Glycerate 2-kinases are involved in the degradation of Glc and other metabolic pathways in animals and bacteria (Guo et al, 2006;Kehrer et al, 2007) but have not been reported for plants. Instead, a glycerate 3-kinase (GLYK) occurs in plant chloroplasts and many cyanobacteria, where it produces glycerate 3-phosphate (3PGA) from glycerate in the last step of the photorespiratory C 2 cycle (Boldt et al, 2005;Bartsch et al, 2008). This pathway is an indispensable auxiliary component of the photosynthetic CO 2 assimilation network in cyanobacteria and plants (Eisenhut et al, 2008), and its operation is most evident in higher plants with the C 3 pathway of photosynthesis.…”

mentioning

confidence: 99%

An Autoinhibitory Domain Confers Redox Regulation to Maize Glycerate Kinase

Bartsch

Mikkat²,

Hagemann

et al. 2010

Plant Physiology

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Glycerate 3-kinase (GLYK) is the terminal enzyme of the photorespiratory cycle in plants and many cyanobacteria. For several C 4 plants, notably grasses of the NADP-malic enzyme (ME) subtype, redox regulation of GLYK has been reported, but the responsible molecular mechanism is not known. We have analyzed the enzyme from the NADP-ME C 4 plant maize (Zea mays) and found that maize GLYK, in contrast to the enzyme from C 3 plants and a dicotyledonous NADP-ME C 4 plant, harbors a short carboxy-terminal extension. In its oxidized (night) form, a disulfide bridge is formed between the two cysteine residues present in this extra domain, and GLYK activity becomes inhibited. Cleavage of this bond by thioredoxin f produces the fully active thiol form, releasing autoinhibition. Fusion of the maize GLYK redox-regulatory domain to GLYK from C 3 plants confers redox regulation to these otherwise unregulated enzymes. It appears that redox regulation of GLYK could be an exclusive feature of monocotyledonous C 4 plants of the NADP-ME type, in which linear electron transport occurs only in the mesophyll chloroplasts. Hence, we suggest that GLYK, in addition to its function in photorespiration, provides glycerate 3-phosphate for the accelerated production of triose phosphate and its export from the mesophyll. This could facilitate the activation of redoxregulated Calvin cycle enzymes and the buildup of Calvin cycle intermediates in the bundle sheath of these particular C 4 plants during the dark/light transition.

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“…Mutations in enzymes of this pathway usually are lethal, underlining the importance of this salvage pathway [2][3][4]. Although all enzymes and some of the metabolite transporters involved in this highly compartmentalized pathway have been identified [5][6][7][8][9], information about the majority of the transport proteins and the processes regulating the pathway is still missing [1,4], possibly because mutations in the corresponding genes cause subtle metabolic phenotypes. Thus, a high-throughput method to quantify metabolites known to accumulate in photorespiratory mutants, glyoxylate and ammonium, is desirable.…”

mentioning

confidence: 99%

“…For glyoxylate quantification, 450 ll of the supernatant is mixed with 50 ll of a freshly prepared 1% (v/v) solution of phenylhydrazine in 100 mM HCl, and the sample is incubated at 95°C for 2 min and cooled on ice for 6 min. The sample is acidified by adding 250 ll of concentrated HCl and is divided into three 225-ll aliquots in cavities of a 96-well plate; two technical replicates are oxidized with 25 ll of a solution of 1.6% (w/v) K 3 Fe(CN) 6 with 25 ll of water added. Color formation is measured exactly 6 min after the addition of K 3 Fe(CN) 6 solution because the reaction reaches a plateau after 4 min and the colored reaction product slowly decomposes with time afterward.…”

mentioning

confidence: 99%

High-throughput colorimetric method for the parallel assay of glyoxylic acid and ammonium in a single extract

Bräutigam

Gagneul

Weber

2007

Analytical Biochemistry

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Glyoxylate and ammonia are signature metabolites of a major plant metabolic pathway, the C 2 oxidative carbon cycle, also known as photorespiration. This complex salvage pathway recycles most of the carbon that is lost from the Calvin cycle in the form of phosphoglycolate as a consequence of the oxygenation reaction of RuBP carboxylase-oxygenase (RuBisCO) 2 and constitutes a significant metabolic flux in photosynthesizing leaves of C 3 plants [1]. Mutations in enzymes of this pathway usually are lethal, underlining the importance of this salvage pathway [2][3][4]. Although all enzymes and some of the metabolite transporters involved in this highly compartmentalized pathway have been identified [5][6][7][8][9], information about the majority of the transport proteins and the processes regulating the pathway is still missing [1,4], possibly because mutations in the corresponding genes cause subtle metabolic phenotypes. Thus, a high-throughput method to quantify metabolites known to accumulate in photorespiratory mutants, glyoxylate and ammonium, is desirable. Here we present improved versions of two colorimetric methods for the quantification of ammonia and glyoxylate that make these procedures suitable for high-throughput and sensitive quantification of these signature metabolites in plant tissues.

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d-GLYCERATE 3-KINASE, the Last Unknown Enzyme in the Photorespiratory Cycle in Arabidopsis, Belongs to a Novel Kinase Family

Cited by 137 publications

References 43 publications

Algal evolution in relation to atmospheric CO ₂ : carboxylases, carbon-concentrating mechanisms and carbon oxidation cycles

Algal evolution in relation to atmospheric CO ₂ : carboxylases, carbon-concentrating mechanisms and carbon oxidation cycles

An Autoinhibitory Domain Confers Redox Regulation to Maize Glycerate Kinase

High-throughput colorimetric method for the parallel assay of glyoxylic acid and ammonium in a single extract

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d-GLYCERATE 3-KINASE, the Last Unknown Enzyme in the Photorespiratory Cycle in Arabidopsis, Belongs to a Novel Kinase Family

Cited by 137 publications

References 43 publications

Algal evolution in relation to atmospheric CO 2 : carboxylases, carbon-concentrating mechanisms and carbon oxidation cycles

Algal evolution in relation to atmospheric CO 2 : carboxylases, carbon-concentrating mechanisms and carbon oxidation cycles

An Autoinhibitory Domain Confers Redox Regulation to Maize Glycerate Kinase

High-throughput colorimetric method for the parallel assay of glyoxylic acid and ammonium in a single extract

Contact Info

Product

Resources

About

Algal evolution in relation to atmospheric CO ₂ : carboxylases, carbon-concentrating mechanisms and carbon oxidation cycles

Algal evolution in relation to atmospheric CO ₂ : carboxylases, carbon-concentrating mechanisms and carbon oxidation cycles