The predicted secondary structures of class I fructose-bisphosphate aldolases
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چکیده
منابع مشابه
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 ...
متن کاملInactivation 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...
متن کاملExtended amino acid sequences around the active-site lysine residue of class-I fructose 1,6-bisphosphate aldolases from rabbit muscle, sturgeon muscle, trout muscle and ox liver.
1. Amino acid sequences covering the region between residues 173 and 248 [adopting the numbering system proposed by Lai, Nakai & Chang (1974) Science 183, 1204-1206] were derived for trout (Salmo trutta) muscle aldolase and for ox liver aldolase. A comparable sequence was derived for residues 180-248 of sturgeon (Acipenser transmontanus) muscle aldolase. The close homology with the rabbit muscl...
متن کاملStructure, function and evolution of the Archaeal class I fructose-1,6-bisphosphate aldolase.
FBPA (fructose-1,6-bisphosphate aldolase) catalyses the reversible aldol condensation of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate to form fructose 1,6-bisphosphate. Two classes of FBPA, which rely on different reaction mechanisms, have so far been discovered, class I mainly found in Eucarya and class II mainly in Bacteria. Only recently were genes encoding proteins with FBPA ac...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1988
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2490789