Isomer activation controls stereospecificity of class I fructose-1,6-bisphosphate aldolases

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The fructose-1,6-bisphosphate aldolases: same reaction, different enzymes.

Two forms of the enzyme fructoseI ,6-bisphosphate aldolase (EC 4. I .2.13) are known, designated class I and class 11. The enzymes o f class I function by imine formation between the substrate and a catalytically essential lysine residue in the active site, which acts to stabilize the intermediate carbanion (for review, see [ I , 21). The enzymes of class I1 utilize a divalent metal ion to act ...

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Inactivation of Class I Fructose Diphosphate Aldolases by the Substrate Analog N-Bromoacetylethanolamine

N-Bromoacetylethanolamine phosphate, prepared by the bromoacetylation of ethanolamine phosphate, has been tested as an active site-specilic reagent for rabbit and rat muscle fructose diphosphate aldolases. The reagent inactivates both enzymes, and inactivation is prevented by substrates or competitive inhibitors. Loss of activity is pseudo-first order until the later stages of inactivation, and...

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Inactivation of class I fructose diphosphate aldolases by the substrate analog N-bromoacetylethanolamine phosphate.

N-Bromoacetylethanolamine phosphate, prepared by the bromoacetylation of ethanolamine phosphate, has been tested as an active site-specilic reagent for rabbit and rat muscle fructose diphosphate aldolases. The reagent inactivates both enzymes, and inactivation is prevented by substrates or competitive inhibitors. Loss of activity is pseudo-first order until the later stages of inactivation, and...

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Immunochemical studies using polyclonal antisera prepared individually against highly purified cytosolic and chloroplast spinach leaf (Spinacia oleracea) fructose bisphosphate aldolases showed significant cross reaction between both forms of spinach aldolase and their heterologous antisera. The individual cross reactions were estimated to be approximately 50% in both cases under conditions of a...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 2017

ISSN: 0021-9258

DOI: 10.1074/jbc.m117.811034