Interaction between Rabbit Muscle Aldolase and Dihydroxyacetone Phosphate
نویسندگان
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...
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A multienzyme system composed by recombinant dihydroxyacetone kinase from Citrobacter freundii, fuculose-1-phosphate aldolase and acetate kinase, allows a practical one-pot C-C bond formation catalysed by dihydroxyacetone phosphate-dependent aldolases from dihydroxyacetone and an aldehyde.
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Dihydroxyacetone phosphate acyl transferase (DHAP-AT), alkyl dihydroxyacetone phosphate synthase (alkyl-DHAP-synthase), and glycerol-3-phosphate acyltransferase (GPAT) activities were investigated under optimal assay conditions using highly purified organelle preparations. The data presented clearly indicate that GPAT activity was mainly localized in mitochondria and microsomes, whereas DHAP-AT...
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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...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1963
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)83969-8