Oxidative Deamination of Amino Acids by Pyridoxal and Metal Salts1

1954 ◽  
Vol 76 (19) ◽  
pp. 4900-4902 ◽  
Author(s):  
Miyoshi Ikawa ◽  
Esmond E. Snell
Keyword(s):  
Amino Acids ◽  
Oxidative Deamination

scholarly journals The Chemical Mechanism of The Oxidative Deamination of Amino Acids by Catechol and PolYPHENOLASE

1950 ◽  
Vol 3 (3) ◽  
pp. 356 ◽  
Author(s):  
EM Trautner ◽  
EAH Roberts
Keyword(s):  
Amino Acids ◽  
Chemical Mechanism ◽  
Secondary Amines ◽  
Oxidative Deamination ◽  
Structural Homologues

The continuous deamination of certain amino acids by the system catecholpolyphenolasetakes place through intensely coloured intermediate compounds.These intermediates are formed by the combination of equimolecular proportionsof o-quinone with amino acids or secondary amines. They are presentedas structural homologues of adrenochrome or hallachrome and probably ofSzent-Gyorgyi's tyrin (1925).

scholarly journals On the formation of amino acids deriving from spermidine and spermine

1981 ◽  
Vol 200 (1) ◽  
pp. 123-132 ◽  
Author(s):  
N Seiler ◽  
B Knödgen ◽  
M W Gittos ◽  
W Y Chan ◽  
G Griesmann ◽  
...  
Keyword(s):  
Amino Acids ◽  
Aldehyde Dehydrogenase ◽  
Oxidative Metabolism ◽  
Spermine Oxidase ◽  
Oxidative Deamination ◽  
Naturally Occurring ◽  
Rats And Mice ◽  
Related Compounds

Evidence obtained from experiments with rats and mice is presented suggesting that the naturally occurring amino acids putreanine and N8-(2-carboxyethyl)spermidine, and most probably also related compounds deriving from the polyamines spermidine and spermine by oxidative metabolism, are formed within two anatomical compartments. In the first step polyamines are converted into aldehydes by serum spermine oxidase in the circulation. A certain portion of these aldehydes can be taken up by liver and other organs and transformed by aldehyde dehydrogenase into the corresponding amino acids. Putreanine is not only derived from spermidine, but can also be formed from N8-(2-carboxyethyl)spermidine by oxidative deamination, catalysed by serum spermine oxidase, and subsequent spontaneous elimination of acrolein.

Pyridoxal- and metal ion-catalyzed oxidative deamination of alpha amino acids

1987 ◽  
Vol 138 (3) ◽  
pp. 231-239 ◽  
Author(s):  
Kuniyasu Tatsumoto ◽  
Masami Haruta ◽  
Arthur E. Martell
Keyword(s):  
Amino Acids ◽  
Metal Ion ◽  
Oxidative Deamination

Effects of hexamethonium and methyl-p-tyrosine on normal rats subjected to convulsions induced by oxygen at high pressure

1980 ◽  
Vol 58 (3) ◽  
pp. 237-242 ◽  
Author(s):  
E. W. Banister ◽  
A. K. Singh
Keyword(s):  
Amino Acids ◽  
High Pressure ◽  
Protective Action ◽  
Latency Period ◽  
Oxygen Toxicity ◽  
Aminobutyric Acid ◽  
Brain Catecholamines ◽  
Oxidative Deamination ◽  
The Brain ◽  
Catecholamine Concentration

Hexamethonium infusion (intravenous) does not alter the concentrations of brain catecholamines, ammonia, and amino acids in rats under normal conditions. However, it decreases the concentration of blood adrenaline (A) and nonadrenaline (NA) significantly without affecting blood ammonia and amino acids. Injection of α-methyl-p-tyrosine (α-MPT) (intraperitoneal) decreases brain catecholamines without affecting the concentration of ammonia and amino acids in the brain or catecholamines, ammonia, and amino acids in the blood.In normal, hexamethonium-, and α-MFT-treated rats convulsed by exposure to oxygen at high pressure (OHP), the concentration of ammonia and glutamine plus aspargine increased and glutamate and γ-aminobutyric acid (GABA) (brain only) decreased significantly in both blood and brain. After convulsion, hexamethonium and α-MPT effect the same degree of concentration change for ammonia and amino acids in both blood and brain.When hexamethonium-treated rats are convulsed by OHP, the concentrations of A and NA in blood increased significantly. However, the postconvulsive concentration of A in these rats is significantly less than the preconvulsive control values of normal, undrugged rats. Hexamethonium also prolongs the latency period before convulsions induced by exposure of rats to OHP. This protective action of hexamethonium against oxygen toxicity is probably due to (a) some direct effect of low circulating catecholamines, or (b) delay in the production of toxic levels of ammonia from oxidative deamination of catecholamines, as initial low catecholamine concentration would hinder accumulation of ammonia from such deamination.α-MPT treatment was ineffective in producing an increased latency period before convulsion occurred despite the prevailing low brain catecholamine initially produced by α-MPT treatment. However, the concentration of brain A, NA, and total catecholamines decreased significantly after α-MPT-treated rats were convulsed by OHP exposure. The response of blood catecholamines to OHP-induced convulsions in these α-MPT-treated rats is the same as in normal rats.As α-MPT blocks the synthesis of catecholamines, a further decrease in brain catecholamine values after oxygen-induced convulsions in drugged animals suggests that brain catecholamines are oxidatively deaminated to produce ammonia. These observations suggest that, contrary to earlier reports, brain catecholamines do play an important role in producing ammonia during oxygen toxicity, which, in turn, induces convulsions.

scholarly journals Identification of an Acidic Amino Acid Permease Involved in d-Aspartate Uptake in the Yeast Cryptococcus humicola

2021 ◽  
Vol 9 (1) ◽  
pp. 192
Author(s):  
Daiki Imanishi ◽  
Yoshio Kera ◽  
Shouji Takahashi
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Yeast Genome ◽  
Acidic Amino Acid ◽  
Oxidative Deamination ◽  
Amino Acid Permease ◽  
Cryptococcus Humicola ◽  
Growth Defects ◽  
Alkaline Conditions ◽  
The Relationship

d-aspartate oxidase (DDO) catalyzes the oxidative deamination of acidic d-amino acids, and its production is induced by d-Asp in several eukaryotes. The yeast Cryptococcus humicola strain UJ1 produces large amounts of DDO (ChDDO) only in the presence of d-Asp. In this study, we analyzed the relationship between d-Asp uptake by an amino acid permease (Aap) and the inducible expression of ChDDO. We identified two acidic Aap homologs, named “ChAap4 and ChAap5,” in the yeast genome sequence. ChAAP4 deletion resulted in partial growth defects on d-Asp as well as l-Asp, l-Glu, and l-Phe at pH 7, whereas ChAAP5 deletion caused partial growth defects on l-Phe and l-Lys, suggesting that ChAap4 might participate in d-Asp uptake as an acidic Aap. Interestingly, the growth of the Chaap4 strain on d- or l-Asp was completely abolished at pH 10, suggesting that ChAap4 is the only Aap responsible for d- and l-Asp uptake under high alkaline conditions. In addition, ChAAP4 deletion significantly decreased the induction of DDO activity and ChDDO transcription in the presence of d-Asp. This study revealed that d-Asp uptake by ChAap4 might be involved in the induction of ChDDO expression by d-Asp.

Sign in / Sign up

Export Citation Format

Share Document