Fructose-1,6-bisphosphate aldolase

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Properties of fructose-1,6-bisphosphate aldolase inactivating enzymes in rat liver lysosomes

Biochimica et Biophysica Acta (BBA) - Enzymology, 1981
The intralysosomal localization of the enzymes that catalyse inactivation of rat liver fructose-bisphosphate aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase, EC 4.1.2.13) to a form with antigenic activity was demonstrated. The inactivating enzymes like all other lysosomal markers tested except acid phosphatase, were readily ...
E, Kominami, S, Hashida, N, Katunuma
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Fructose-1,6-bisphosphate aldolase of Mycoplasma bovis is a plasminogen-binding adhesin

Microbial Pathogenesis, 2018
Mycoplasma bovis is an extremely small cell wall-deficient pathogenic bacterium in the genus Mycoplasma that causes serious economic losses to the cattle industry worldwide. Fructose-1,6-bisphosphate aldolase (FBA), a key enzyme in the glycolytic pathway, is a multifunctional protein in several pathogenic bacterial species, but its role in M.
Xiang, Gao +7 more
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Properties of Fructose-1,6-Bisphosphate Aldolase from Escherichia coli: An NMR Analysis

Archives of Biochemistry and Biophysics, 1995
A class II Zn(2+)-dependent fructose-1,6-bisphosphate (FBP)- aldolase was purified from an overproducer strain of Escherichia coli and characterized by standard biochemical techniques and 13C NMR spectroscopy. The principal finding of these studies was identification, by 13C NMR spectroscopy, of an enzyme-bound reaction intermediate, the enediol(ate ...
B S, Szwergold, K, Ugurbil, T R, Brown
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Fructose-1,6-bisphosphate aldolase

2021
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Cloning and characterization of Leishmania mexicana fructose-1,6-bisphosphate aldolase