Molecular Cloning, Expression, Purification, and Characterization of Fructose-1,6-bisphosphate Aldolase from Thermus aquaticus

2001 ◽  
Vol 21 (2) ◽  
pp. 293-302 ◽  
Author(s):  
Véronique Sauvé ◽  
Jurgen Sygusch
Keyword(s):  
Molecular Cloning ◽  
Purification And Characterization ◽  
Thermus Aquaticus ◽  
Fructose 1,6 Bisphosphate

scholarly journals Molecular Cloning of groESL Locus, and Purification and Characterization of Chaperonins, GroEL and GroES, from Bacillus brevis

2001 ◽  
Vol 65 (6) ◽  
pp. 1379-1387 ◽  
Author(s):  
Masao TOKUNAGA ◽  
Yoichi SHIRAISHI ◽  
Masatake ODACHI ◽  
Makoto MIZUKAMI ◽  
Hiroko TOKUNAGA ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Purification And Characterization ◽  
Bacillus Brevis

scholarly journals Purification and characterization of the class-II D-fructose 1,6-bisphosphate aldolase from Escherichia coli (Crookes' strain)

1978 ◽  
Vol 169 (3) ◽  
pp. 633-641 ◽  
Author(s):  
S A Baldwin ◽  
R N Perham ◽  
D Stribling
Keyword(s):  
Escherichia Coli ◽  
Common Ancestor ◽  
Class Ii ◽  
Purification And Characterization ◽  
Thiol Compounds ◽  
E Coli ◽  
Optimum Ph ◽  
Class Ii Aldolase ◽  
Fructose 1,6 Bisphosphate

A new form of the class-II D-fructose 1,6-bisphosphate aldolase (EC 4.1.2.13) of Escherichia coli (Crookes' strain) was isolated from an extract of glycerol-grown bacteria. It has a higher molecular weight (approx. 80000)than previous preparations of the enzyme and closely resembles the typical class-II aldolase from yeast in size and amino acid composition. On the other hand, its kinetic behaviour is not typical of a class-II aldolase. The enzyme has no requirement for thiol compounds either for stability or activity, added K+ ions have no effect, and the optimum pH for the cleavage activity is unusually high. The class-II enzymes from the prokaryote E. coli and the eukaryote yeast show no immunological identity. However, the similarity of their structures suggests that they have evolved from a common ancestor.

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