Class I aldolases: Substrate specificity, mechanism, inhibitors and structural aspects
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چکیده
منابع مشابه
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...
متن کاملInactivation 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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Background & Aims: A successful treatment in the field of medical sciences depends on an accurate diagnosis. In orthodontic diagnosis and treatment planning also analyzing the sagittal jaw base relationship is important. Various methods have been suggested for this. This study aimed to investigate the accuracy of beta angle in sagittal jaw base relationship diagnosis. Materials & Methods: In t...
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Tagatose-1,6-bisphosphate aldolase (TBPA) is a tetrameric class II aldolase that catalyzes the reversible condensation of dihydroxyacetone phosphate with glyceraldehyde 3-phosphate to produce tagatose 1,6-bisphosphate. The high resolution (1.45 A) crystal structure of the Escherichia coli enzyme, encoded by the agaY gene, complexed with phosphoglycolohydroxamate (PGH) has been determined. Two s...
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ژورنال
عنوان ژورنال: Progress in Biophysics and Molecular Biology
سال: 1995
ISSN: 0079-6107
DOI: 10.1016/0079-6107(95)00008-9