Fructose diphosphate aldolase-Class I (Schiff base) from Mycobacterium tuberculosis H37Rv.
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Date
1981-12
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Abstract
An aldolase was partially purified from fermenter grown Mycobacterium tuberculosis
H37Rv cells. The aldolase has a molecular weight of 150,000, possesses a tetrameric
structure and cleaves both fructose diphosphate and fructose- 1-phosphate, the former being
cleaved 17 times faster. The enzyme was inactivated by treatment with NaBH4 in the presence
of fructose diphosphate or dihydroxyacetone, phosphate suggesting Schiff base formation
during its catalytic function. Thiol reagents, EDTA and metal ions had no apparent effect on
the aldolase activity. These results show that aldolase is of Class I type. However, this
enzyme, unlike the mammalian Class I aldolase, was unaffected by carboxypeptidase A. Nethylmaleiniide
and dithionitrobenzoic acid.
Description
Keywords
Mycobacterium tuberculosis, fructose biphosphate, aldolase, Schiff base Class I
Citation
Bai N Jayanthi, Pai M Ramachandra, Murthy P Suryanarayan, Venkatasubramanian T A. Fructose diphosphate aldolase-Class I (Schiff base) from Mycobacterium tuberculosis H37Rv. Journal of Biosciences. 1981 Dec; 3(4): 323-332.