Aldolase crystalline

H. P. Meloche, J. M. Ingram, and W. A. Wood, 2-Keto-3-deoxy-6-phosphogluconic aldolase (crystalline). Methods Enzymol. 9 520 (1966). 

D-afe-o-Heptulose (sedoheptulose) (XXXVII) has been synthesized from D-erythrose (XXXVIII) plus triose phosphate, using an aldolase preparation from peas.169 Aldolases from yeast and from rat liver also form heptu-lose phosphate from these substrates.7S(o) 170(a) Crystalline muscle aldolase causes the formation of L-jrZwco-heptulose (XXXVIIa) from a mixture of L-erythrose (XXXVTIIa) and hexose diphosphate.170(b)... 

The maintenance within a recognizable range of the serum enzyme activities implies some similarity between their rate of discharge from the tissues into the blood stream and the rapidity of their clearance from it. This clearance can be exceedingly swift, though confronted by skeletal muscle of which 300 mg contains as much aldolase as the entire adult circulation (S22). After the intravenous injection of crystalline aldolase in rats the activity of the serum aldolase rises 7-fold in the first 15 minutes, but 12 hours later has fallen to only 1.5 times the normal value (S24). Further, the intravenous injection in rabbits of pure crystalline aldolase labeled with and the measurement of the rate of disappearance of radioactivity in successive serum specimens indicate... 

Some properties of this crystalline material have been investigated (Henrotte, 1954). Its molecular weight is 67,000, thus differing very much from the values of 160,(XX) of rabbit myogen A and B (Gralen, 1939 Bailey, 1940) it has no aldolase or phosphoglyceraldehyde dehydrogenase activities, and its function in the metabolism of the cell is still unknown. 

There are some oligomeric proteins—for instance a-crystallin [47] and high-density lipoprotein [48J—which did not dissociate into subunits, though 90% of lysyl residues were succinylated. Succinylation of aldolase [40] and ceruloplasmin [43] in neutral solution led to intermediary subunits only, whereas the final dissociation into the... 

We have recently overexpressed a fuculose 1-phosphate (Fuc-l-P) aldolase from E. coli and have begun to evaluate its utility as a catalyst for carbohydrate synthesis (24). We have expressed the enzyme using a tac promoter, to a level of 6 X 10 units per liter (one unit of enzyme catalyzes the conversion of 1 pmol of substrates to products per minute under optimal conditions of temperature and pH). The enzyme is easily purified to crystallinity using ion-exchange chromatography. Fuc-l-P aldolase has a usefully broad substrate specificity, at least with regard to the electrophilic component the enzyme appears to accept over 40 compounds in kinetic... 

Like lactic dehydrogenase, aldolase exists in multiple forms, the existence of which were not immediately obvious on electrophoresis. Electrophoresis of crystalline aldolase yields a single but rather broad band, and only through electrofocusing were five different forms of the enzyme discovered. 

Aldolase has been crystallized from muscle by various methods. The crystalline enzyme is quite specific for the dihydroxyacetone portion of the molecule, but very nonspecific for the aldehyde. The only structure... 

This apparent controversy was resolved by the seminal work of David Gutsche who developed reproducible synthetic procedures for the family of vase-like compounds, which in 1975 he called Calixarenes. David became interested in the chemistry of the Zinke compounds because he was a consultant to the Petrolite Corporation that produced surfactants for the oil industry. One of their products was a linear ohgomer obtained from reaction of p-tert-butylphenol and formaldehyde. Problems in the production process led to a detailed study of the reaction and during the more detailed investigations the Petrolite team rediscovered the crystalline Zinke compound. David s personal interest in these macrocyclic molecules was their possible use as platforms for enzyme mimics, in particular the Aldolase catalysis. Although he never realized such an artificial enzyme, David devoted... 

Meyerhof, O., Lohmann, K., and Schuster, P., Biochem. Z., 286, 301, 319 (1936). It has recently been reported that the classical crystalline muscle aldolase has no action on fructose-l-phosphate. The reaction described in Fig. 1 is stated to be catalyzed by a 1-phosphofructaldosase found in liver. (Leuthardt, F., Testa, E., and Wolf, H. P., Heh. Chim. Acta 36, 227 (1953).)... 

Aldolase is found in relatively high concentrations in muscle. It has been prepared in crystalline form, and its molecular weight is 150,000. It is activated by bivalent ions. 

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