The Thermal Inactivation of Acetoacetate Decarboxylase
نویسندگان
چکیده
منابع مشابه
Stereochemical Course of the Decarboxylation Catalyzed by Acetoacetate Decarboxylase
The stereochemical course of the decarboxylation of acetoacetate catalyzed by the enzyme acetoacetate decarboxylase (AAD) has been studied by using samples of optically active 2-tritioacetoacetate, prepared by enzymatic oxidation of samples of enantiomeric pairs of diastereomeric 2-tritio-3-hydroxybutyrates. A correlation is proposed connecting the stereochemical course of enzymatic decarboxyla...
متن کاملOrigin of the pKa shift of the catalytic lysine in acetoacetate decarboxylase.
The pKa value of Lys115, the catalytic residue in acetoacetate decarboxylate, was calculated using atomic coordinates of the X-ray crystal structure with consideration of the protonation states of all titratable sites in the protein. The calculated pKa value of Lys115 (pKa(Lys115)) was unusually low (approximately 6) in agreement with the experimentally measured value. Although charged residues...
متن کاملThe interactions of acetoacetate decarboxylase with carbonyl compounds, hydrogen cyanide, and an organic mercurial.
1. Hydrogen cyanide inhibited acetoacetate decarboxylase only when incubated with the enzyme in the presence of car-bony1 compounds. This resulted in an inhibitory synergism between hydrogen cyanide and carbonyl compounds. This synergism was used to investigate the comparative abilities of various carbonyl compounds to form Schiff’s bases at the active site of the enzyme. The order of effective...
متن کاملCloning, sequencing, and molecular analysis of the acetoacetate decarboxylase gene region from Clostridium acetobutylicum.
Acetoacetate decarboxylase (ADC) (EC4.1.1.4) of Clostridium acetobutylicum DSM 792 was purified to homogeneity, and its first 25 N-terminal amino acids were determined. Oligonucleotide probes deduced from this sequence were used to detect positive clones in partial gene banks derived from Sau3A and HaeIII digests with following ligation into the vector pUC9. In Escherichia coli, the 2.1-kbp Hae...
متن کاملThe mechanism of acetoacetate synthesis.
The observation of a coenayme A (CoA)-catalyzed acetoacetate synthesis from acetate and adenosinetriphosphate in pigeon liver extracts (1) grouped this reaction with the larger family of acetylation reactions. Furthermore it furnished partial confirmation of an earlier calculation (2) showing that 16,000 calories are required for the condensation of two acetates to acetoacetate. Thus, one energ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1970
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)62744-9