The Enzymatic Synthesis of Holotranscarboxylase from Apotranscarboxylase and (+)-Biotin
Open Access
- 1 September 1964
- journal article
- Published by Elsevier
- Vol. 239 (9), 2865-2871
- https://doi.org/10.1016/s0021-9258(18)93826-3
Abstract
No abstract availableThis publication has 16 references indexed in Scilit:
- Biotin- and adenosine triphosphate-dependent activation of propionyl apocarboxylaseBiochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1963
- Propionyl-CoA holocarboxylase synthesis from biotinyl adenylate and the apocarboxylase in the presence of an activating enzymeBiochemical and Biophysical Research Communications, 1963
- THE BIOCHEMICAL FUNCTION OF BIOTIN, VI. CHEMICAL STRUCTURE OF THE CARBOXYLATED ACTIVE SITE OF PROPIONYL CARBOXYLASEProceedings of the National Academy of Sciences, 1963
- Propionyl holocarboxylase formation: Covalent bonding of biotin to apocarboxylase lysyl ϵ-amino groupsBiochemical and Biophysical Research Communications, 1962
- Propionyl apocarboxylase activation catalyzed by cell-free enzyme extractsBiochemical and Biophysical Research Communications, 1961
- Chemical Synthesis and Properties of Butyryl Adenylate1Journal of the American Chemical Society, 1956
- Spectrophotometric Determination of Vicinal GlycolsAnalytical Chemistry, 1954
- Some reactions of adenosine and inosine phosphates in animal tissuesBiochimica et Biophysica Acta, 1953
- Synthese von S‐β‐Oxybutyryl‐ und S‐Acetacetyl‐Coenzym AAngewandte Chemie, 1953
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934