Arginine as the C-1 phosphate binding site in rabbit muscle aldolase
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چکیده
منابع مشابه
Interaction between rabbit muscle aldolase and dihydroxyacetone phosphate.
It is generally accepted that the mechanism of enzyme activity includes a combination of enzyme and substrate. This concept forms the basis for the conventional kinetic analyses of enzymatic reactions (1). Direct evidence for the existence of enzyme-substrate combinations is as yet meager. The binding of pyridine nucleotide coenzymes as substrates to various dehydrogenases has been shown to res...
متن کاملGram scale synthesis of 3-fluoro-1-hydroxyacetone phosphate: a novel donor substrate in rabbit muscle aldolase-catalyzed aldol reactions.
An efficient gram scale synthesis of 3-fluoro-1-hydroxyacetone phosphate (FHAP) has been developed. As a close analog to dihydroxyacetone phosphate, FHAP was used as a novel donor substrate for rabbit muscle aldolase catalyzed reactions. The different binding affinities of the gem-diol and keto form of FHAP were studied by (19)F-NMR.
متن کاملAmino acid sequence of a fragment of rabbit muscle aldolase.
Cleavage of rabbit muscle aldolase by cyanogen bromide results in the formation of four fragments of different size [1]. Study of the primary structure of the enzyme has been based on the examination of these fragments [1, 2]. Because of the insolubility and associated problems due to the relatively large size of the fragments Lai [1], as well as Anderson et al. [3], used pyridine-acetic acid b...
متن کاملD-Serine dehydratase from Escherichia coli. Essential arginine residue at the pyridoxal 5'-phosphate binding site.
D-Serine apodehydratase from Escherichia coli is rapidly inactivated by butanedione in K+ borate buffer or by phenylglyoxal in K+ phosphate buffer at pH 8, 25 degrees. Pyridoxal-P protects against the inactivation. Modification of the apoenzyme abolishes its ability to bind the cofactor, pyridoxal-P, but the apparent Km for the substrate, D-serine, is not altered. The concentration dependence o...
متن کاملSubstrate-induced dissociation of rabbit muscle aldolase into active subunits.
For several years, data have been presented which suggested that the enzyme aldolase, from rabbit muscle, is composed of three subunits of identical, or nearly identical, size and structure (Drechsler et al 1959; Kowalsky -A, and Bayer, 1960; Schachman, 1960; Stellwagen and Schachman, 1962; Deal e al,,19653 Rutter et al 1965; and Winstead and Wold, 1964). More recent 3 data, however, indicate t...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1975
ISSN: 0014-5793
DOI: 10.1016/0014-5793(75)81070-2