NDLI: Identification of arginine 331 as an important active site residue in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli.

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Identification of arginine 331 as an important active site residue in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli.

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Identification of arginine 331 as an important active site residue in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Qamar, S. Berry, A. Marsh, K.
Description	Country affiliation: United kingdom Author Affiliation: Qamar S ( Department of Biochemistry, University of Cambridge, United Kingdom.)
Abstract	Treatment of the Class II fructose-1,6-bisphosphate aldolase of Escherichia coli with the arginine-specific alpha-dicarbonyl reagents, butanedione or phenylglyoxal, results in inactivation of the enzyme. The enzyme is protected from inactivation by the substrate, fructose 1,6-bisphosphate, or by inorganic phosphate. Modification with [7-14C] phenylglyoxal in the absence of substrate demonstrates that enzyme activity is abolished by the incorporation of approximately 2 moles of reagent per mole of enzyme. Sequence alignment of the eight known Class II FBP-aldolases shows that only one arginine residue is conserved in all the known sequences. This residue, Arg-331, was mutated to either alanine or glutamic acid. The mutant enzymes were much less susceptible to inactivation by phenylglyoxal. Measurement of the steady-state kinetic parameters revealed that mutation of Arg-331 dramatically increased the K(m) for fructose 1,6-bisphosphate. Comparatively small differences in the inhibitor constant Ki for dihydroxyacetone phosphate or its analogue, 2-phosphoglycolate, were found between the wild-type and mutant enzymes. In contrast, the mutation caused large changes in the kinetic parameters when glyceraldehyde 3-phosphate was used as an inhibitor. Kinetic analysis of the oxidation of the carbanionic aldolase-substrate intermediate of the reaction by hexacyanoferrate (III) revealed that the K(m) for dihydroxyacetone phosphate was again unaffected, whereas that for fructose 1,6-bisphosphate was dramatically increased. Taken together, these results show that Arg-331 is critically involved in the binding of fructose bisphosphate by the enzyme and demonstrate that it interacts with the C-6 phosphate group of the substrate.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	1
Volume Number	5
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1996-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Arginine Chemistry Escherichia Coli Enzymology Fructose-bisphosphate Aldolase Amino Acid Sequence Metabolism Binding Sites Antagonists & Inhibitors Genetics Kinetics Molecular Sequence Data Mutagenesis, Site-directed Oligodeoxyribonucleotides Oxidation-reduction Sequence Homology, Amino Acid Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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