Formation and Breakdown of Amino-acids by Inter-molecular Transfer of the Amino Group

  title={Formation and Breakdown of Amino-acids by Inter-molecular Transfer of the Amino Group},
  author={A. Braunstein and M. Kritzmann},
WE have previously reported1 the discovery in muscle of a highly active metabolic mechanism, by the action of which the amino group and two hydrogen atoms of glutamic acid are transferred to pyruvic acid (added or of metabolic origin) with the formation of alanine (and ketoglutaric acid). This is the key to the puzzling fact that glutamic acid is transformed into succinic acid by muscle tissue without the formation of either ammonia or amide nitrogen (D. Moyle-Needham). 
The degradation of amino-acids
Amino-acids may (1) be utilised in protein synthesis either by being linked together through the synthesis of peptide bonds or, as now seems less likely, by acting as a nitrogen pool for proteinExpand
Transamination and the integrative functions of the dicarboxylic acids in nitrogen metabolism.
  • A. Braunstein
  • Chemistry, Medicine
  • Advances in protein chemistry
  • 1947
The conception of the dicarboxylic acid system as a central component of first order in the chemical integration of nitrogenous metabolism satisfactorily accounts for the widespread occurrence of transamination and for its exceptionally high activity in certain tissues. Expand
Deamination of Nucleotides and the Role of their Deamino Forms in Ammonia Formation from Amino Acids
Conway and Cooke, studying the deamination of adenosine and of AMP in various tissues, demonstrated that they were also deaminated by brain tissue.(1) In 1953 Muntz(2) showed that in acetone powderExpand
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The discovery of enzymatic transamination was one of the remarkable events in the history of biochemistry of our century. Like all genuine discoveries, it was more or less accidental andExpand
L-Glutamate-L-amino acid transaminases.
This chapter discusses the assays for various glutamate (α-ketoglutarate)-utilizing transaminases for comparative purposes and their purification and assay procedures. Expand
Transaminases for the synthesis of enantiopure beta-amino acids
This review gives an overview over microbial transaminases with activity towards β-amino acids and their substrate spectra and outlines current strategies for the screening of new biocatalysts. Expand
Properties of bacterial and archaeal branched-chain amino acid aminotransferases
The structure-function features and the substrate specificity of bacterial and archaeal BCATs differ from eukaryotic ones in the wide substrate specificity, optimal tempera- ture, and reactivity toward pyruvate as the second substrate. Expand
Historical Introduction: The Origin and Growth of Our Present Concepts of Protein Metabolism
Publisher Summary This chapter presents the origin and growth of the present concepts of protein metabolism. Protein is the most abundant nitrogenous compound in the diet and in the body.Expand
2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli.
The three-dimensional structure of a mutant of the aspartate aminotransferase from Escherichia coli, in which the active-site lysine has been substituted by alanine (K258A), has been determined atExpand
Imine Reductases: A Comparison of Glutamate Dehydrogenase to Ketimine Reductases in the Brain
The current review briefly discusses the metabolic importance of the GDH reaction in liver and brain, the mechanistic similarities between GDH and the ketimine reductases, the metabolic significance of the brain ketimines in nitrogen and intermediary metabolism, and the neurochemical consequences of defective ketimin reductase. Expand