Purification of the Glyoxylate Cycle Enzyme Malate Synthase from Maize (Zea mays L) and Characterization of a Proteolytic Fragment

Khan, A. Salam; Vandriessche, E; Kanarek, Louis; Beeckmans, Sonia

doi:10.1006/prep.1993.1068

Cited by 12 publications

(20 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We performed a migration experiment on free pig fumarase and the cytoplasmic isoenzymes of pig malate dehydrogenase and pig aspartate aminotransferase through immobilized isocitrate lyase and malate synthase. The latter four enzymes all have PI values around 5 (Khan et al, 1992(Khan et al, , 1993. As can be seen from Fig.…”

Section: Specificity Of the Associationsmentioning

confidence: 73%

“…Isocitrate lyase (Khan et al, 1992) and malate synthase (Khan et al, 1993) were purified from maize scutella as described before.…”

Section: Enzymes and Enzyme Immobilizationmentioning

confidence: 99%

“…4). Both isocitrate lyase (Khan et al, 1992) and malate synthase (Khan et al, 1993) have been reported to be quite hydrophobic proteins, a property they have in common with serum albumin. Here again, no adsorption whatsoever was detected.…”

Section: Specificity Of the Associationsmentioning

confidence: 99%

“…The latter organism is the subject of our investigations. A simple and high-yield purification procedure was recently developed by us for both isocitrate lyase (Khan et al, 1992) and malate synthase (Khan et al, 1993) from maize scutella, two enzymes which are exclusively confined to the glyoxylate cycle.…”

mentioning

confidence: 99%

See 3 more Smart Citations

A Specific Association Between the Glyoxylic‐Acid‐Cycle Enzymes Isocitrate Lyase and Malate Synthase

Beeckmans

Khan

Driessche

et al. 1994

European Journal of Biochemistry

View full text Add to dashboard Cite

There is accumulating evidence that metabolic pathways are organized in vivo as multienzyme clusters or metabolons. To assess interactions between consecutive enzymes of a pathway in vitro, it is usually essential to modify the physical properties of water around the enzymes, e.g. by immobilizing the latter onto a solid support. Such immobilized enzyme preparations can be embedded in agarose gels and used for affinity electrophoresis [Beeckmans, S., Van Driessche, E. & Kanarek, L. Cell. Biochem. 43, In this study we use the aforementioned technique to investigate the association between two plant glyoxylic acid cycle enzymes, i.e. isocitrate lyase and malate synthase. A specific histochemical staining technique is described for both enzymes. Affinity electrophoresis using either isocitrate lyase or malate synthase as the immobilized enzyme clearly shows that associations are formed between both enzymes. Moreover, experiments with metabolically unrelated enzymes prove that the observed interaction is specific.In recent years it was realized that the aqueous-phase properties in the interior of a cell seem to be essentially different from those of an ordinary aqueous solution (Beeckmans et al

show abstract

Section: Specificity Of the Associationsmentioning

confidence: 73%

“…Isocitrate lyase (Khan et al, 1992) and malate synthase (Khan et al, 1993) were purified from maize scutella as described before.…”

Section: Enzymes and Enzyme Immobilizationmentioning

confidence: 99%

Section: Specificity Of the Associationsmentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

A Specific Association Between the Glyoxylic‐Acid‐Cycle Enzymes Isocitrate Lyase and Malate Synthase

Beeckmans

Khan

Driessche

et al. 1994

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…Although MS has been puriˆed and characterized from a number of plant species, [14][15][16] bacteria, [17][18][19] and yeasts, 20,21) no report has described the puriˆcation and characterization of MS from any basidiomycetous fungi. Because the GLOX cycle enzymes have been shown to play an important role in oxalate biosynthesis in wood-rotting basidiomycetes, we have been motivated to investigate characteristics of the puriˆed enzyme.…”

mentioning

confidence: 99%

Purification and Characterization of Malate Synthase from the Glucose-grown Wood-rotting BasidiomyceteFomitopsis palustris

Munir

Hattori

Shimada

2002

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

Malate synthase (EC 4.1.3.2), the key enzyme of the glyoxylate cycle, was puriˆed to a homogeneous protein from the wood-rotting basidiomycete Fomitopsis palustris grown on glucose. The puriˆed enzyme, with a molecular mass of 520 kDa, was found to consist of eight 65-kDa subunits, and to have K m of 45 and 2.2 mM for glyoxylate and acetyl-CoA, respectively. The enzyme activity was competitively inhibited by oxalate (K i , 8.5 mM) and glycolate (K i , 17 mM), and uncompetitively by coenzyme A (K i , 100 mM). The potent inhibition of the activity by p-chloromercuribenzoate suggests that the enzyme has a sulfhydryl group at the active center. However, the enzyme was inhibited moderately by adenine nucleotides and weakly by some of the metabolic intermediates of glycolysis and tricarboxylic acid cycle. The enzyme was completely inactive in the absence of metal ions and was maximally activated by Mg 2+ (K m , 0.4 mM), which also served to signiˆcantly prevent enzyme inactivation during storage.

show abstract

Malate synthase

Springer Handbook of Enzymes

View full text Add to dashboard Cite

Purification of the Glyoxylate Cycle Enzyme Malate Synthase from Maize (Zea mays L) and Characterization of a Proteolytic Fragment

Cited by 12 publications

References 0 publications

A Specific Association Between the Glyoxylic‐Acid‐Cycle Enzymes Isocitrate Lyase and Malate Synthase

A Specific Association Between the Glyoxylic‐Acid‐Cycle Enzymes Isocitrate Lyase and Malate Synthase

Purification and Characterization of Malate Synthase from the Glucose-grown Wood-rotting BasidiomyceteFomitopsis palustris

Malate synthase

Contact Info

Product

Resources

About