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Directed Evolution of Aldolases
2004Publisher Summary This chapter describes the directed evolution of aldolases. The detailed protocols for generating aldolases with new catalytic properties are presented. The gene encoding aldolase can be amplified using the standard polymerase chain reaction (PCR) from a genomic DNA preparation using the Qiagen kit and primers flanking the gene with
Dirk, Franke +2 more
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The aldolases of chlamydomonas reinhardii
Archives of Biochemistry and Biophysics, 1971The unicellular green alga Chlamydomonas reinhardii contains two distinct aldolases (fructose-1, 6-diphosphate D -glyceraldehyde-3-phosphate-lyase, EC 4.1.2.13). These two enzymes are synthesized under different growth conditions: the alga can contain aldolase I or aldolase II or both of them. The two proteins are localized in the cytoplasm and they
A M, Guerrini, T, Cremona, E C, Preddie
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Rinsho byori. The Japanese journal of clinical pathology, 2002
Aldolase (EC 4.1.2.13) plays an important role in glucose metabolism. Aldolase has a molecular weight of 160 kDa and has three isozymes, namely aldolase A, B and C. The enzyme is probably present in all cells; it occurs in particularly large quantities in the muscles, liver and brain. An increase in serum aldolase is found in myotonic muscular disease,
K, Taguchi, Y, Takagi
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Aldolase (EC 4.1.2.13) plays an important role in glucose metabolism. Aldolase has a molecular weight of 160 kDa and has three isozymes, namely aldolase A, B and C. The enzyme is probably present in all cells; it occurs in particularly large quantities in the muscles, liver and brain. An increase in serum aldolase is found in myotonic muscular disease,
K, Taguchi, Y, Takagi
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Aldolase in Trichomonas vaginalis
Experimental Parasitology, 1955Abstract Sonic homogenates of Trichomonas vaginalis contain a metal activated aldolase. Of the common metal ions studied cobaltous is most effective and ferrous is somewhat less effective. Their action is greatly enhanced by cysteine or thioglycolate. Ethylenediaminetetraacetate is more effective as inhibitor than dipyridyl at pH 7. The inhibition
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Predicted structure for aldolase
Journal of Molecular Biology, 1976Abstract Recent chromatographic and absorbance spectral measurements using the dye Cibacron blue F3GA (Stellwagen et al., 1975) have indicated that the substrate-binding site of fructose diphosphate aldolase is constructed by a supersecondary structural array closely resembling the NAD-domain commonly found in a variety of glycolytic enzymes ...
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Zeitschrift f�r Krebsforschung, 1959
The enzyme aldolase is isolated and crystallized from human breast tumor. The purification of the enzyme involved methanol fractionation, exposure to a temperature of 38°C, adsorption and elution from aluminium hydroxide gel, and precipitation followed by crystallization from ammonium sulfate.
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The enzyme aldolase is isolated and crystallized from human breast tumor. The purification of the enzyme involved methanol fractionation, exposure to a temperature of 38°C, adsorption and elution from aluminium hydroxide gel, and precipitation followed by crystallization from ammonium sulfate.
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Aldolase activity of serum albumins
Organic & Biomolecular Chemistry, 2011Bovine and human serum albumins catalyze the aldol reaction of aromatic aldehyedes and acetone, with saturation kinetics and moderate and opposite enantioselectivity. The reaction occurs at the binding site in domain IIa, and is inhibited by warfarin. Kinetic data are consistent with an enamine mechanism.
BENEDETTI, FABIO +2 more
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European Journal of Cancer (1965), 1966
Abstract There are two different types of aldolase in mammalian tissues, the main difference between these isozymes is the relative activity towards the second substrate of aldolase, fructose- 1 -phosphate (F- 1 -P). In normal liver the ratio of the activities towards fructose di-phosphate (F-d-P) and towards fructose- 1 -phosphate, is near 1 ...
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Abstract There are two different types of aldolase in mammalian tissues, the main difference between these isozymes is the relative activity towards the second substrate of aldolase, fructose- 1 -phosphate (F- 1 -P). In normal liver the ratio of the activities towards fructose di-phosphate (F-d-P) and towards fructose- 1 -phosphate, is near 1 ...
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Characteristics of aldolase variformity
Biochemical and Biophysical Research Communications, 1967Variant heteromorph characteristics in some vertebrate tissues, noting aldolase enzyme anomalous behavior in chicken liver and ...
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