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={Alexander E. Braunstein and M. G. 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 protein

Deamination of Nucleotides and the Role of their Deamino Forms in Ammonia Formation from Amino Acids

Using purified preparations of AMP deaminase of dog brain, Mendicino and Muntz studied the specific activation of the enzyme by ATP and showed that the ATP remained unchanged at the end of the reaction.

The Discovery of Enzymatic Transamination and its Biological Significance

The discovery of enzymatic transamination was one of the remarkable events in the history of biochemistry of the authors' century and was preceded by reports concerning two unrelated processes of tissue metabolism.

L-Glutamate-L-amino acid transaminases.

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.

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.

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 at

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.