Fructose diphosphate aldolase-class I (Schiff base) fromMycobacterium tuberculosis H37Rv |
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Authors: | N Jayanthi Bai M Ramachandra Pai P Suryanarayan Murthy T A Venkitasubramanian |
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Institution: | (1) Department of Biochemistry, Vallabhai Patel Chest Institute, University of Delhi, 110 007 Delhi |
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Abstract: | An aldolase was partially purified from fermenter grownMycobacterium 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. N-ethylmaleiniide
and dithionitrobenzoic acid. |
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Keywords: | Mycobacterium tuberculosis fructose biphosphate aldolase Schiff base Class I |
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