Biosynthesis of alkaloids. On the oxidative deamination of biogenetically important amino acids in papaver somniferum plants

1965 ◽  
Vol 52 (13) ◽  
pp. 395-396 ◽  
Author(s):  
P. Kov�cs ◽  
A. Jindra
Keyword(s):  
Amino Acids ◽  
Papaver Somniferum ◽  
Oxidative Deamination

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

Studies on poppy seed (papaver somniferum) part I: Free amino acids

1965 ◽  
Vol 52 (18) ◽  
pp. 516-517 ◽  
Author(s):  
Ajit Singh Bhown ◽  
Dinesh K. Shah ◽  
Som Nath
Keyword(s):  
Amino Acids ◽  
Free Amino Acids ◽  
Free Amino ◽  
Papaver Somniferum ◽  
Poppy Seed

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 Construction of anti-codon table of the plant kingdom and evolution of tRNA selenocysteine (tRNASec)

BMC Genomics ◽  
2020 ◽  
Vol 21 (1) ◽  
Author(s):  
Tapan Kumar Mohanta ◽  
Awdhesh Kumar Mishra ◽  
Abeer Hashem ◽  
Elsayed Fathi Abd_Allah ◽  
Abdul Latif Khan ◽  
...  
Keyword(s):  
Amino Acids ◽  
Zea Mays ◽  
Amino Acid ◽  
Codon Usage ◽  
Synonymous Codon ◽  
Protein Translation ◽  
Synonymous Codon Usage ◽  
Papaver Somniferum ◽  
Plant Kingdom ◽  
Ostreococcus Tauri

Abstract Background The tRNAs act as a bridge between the coding mRNA and incoming amino acids during protein translation. The anti-codon of tRNA recognizes the codon of the mRNA and deliver the amino acid into the protein translation chain. However, we did not know about the exact abundance of anti-codons in the genome and whether the frequency of abundance remains same across the plant lineage or not. Results Therefore, we analysed the tRNAnome of 128 plant species and reported an anti-codon table of the plant kingdom. We found that CAU anti-codon of tRNAMet has highest (5.039%) whereas GCG anti-codon of tRNAArg has lowest (0.004%) abundance. However, when we compared the anti-codon frequencies according to the tRNA isotypes, we found tRNALeu (7.808%) has highest abundance followed by tRNASer (7.668%) and tRNAGly (7.523%). Similarly, suppressor tRNA (0.036%) has lowest abundance followed by tRNASec (0.066%) and tRNAHis (2.109). The genome of Ipomoea nil, Papaver somniferum, and Zea mays encoded the highest number of anti-codons (isoacceptor) at 59 each whereas the genome of Ostreococcus tauri was found to encode only 18 isoacceptors. The tRNASec genes undergone losses more frequently than duplication and we found that tRNASec showed anti-codon switch during the course of evolution. Conclusion The anti-codon table of the plant tRNA will enable us to understand the synonymous codon usage of the plant kingdom and can be very helpful to understand which codon is preferred over other during the translation.

scholarly journals Construction of Anti-codon Table of the Plant Kingdom and Evolution of tRNA Selenocysteine (tRNAsec)

2020 ◽  
Author(s):  
Tapan Kumar Kumar Mohanta ◽  
Awdhesh Kumar Mishra ◽  
Abeer Hashem ◽  
Elsayed Fathi Abd_Allah ◽  
Ahmed Al-Harrasi
Keyword(s):  
Amino Acids ◽  
Zea Mays ◽  
Amino Acid ◽  
Codon Usage ◽  
Synonymous Codon ◽  
Protein Translation ◽  
Synonymous Codon Usage ◽  
Papaver Somniferum ◽  
Plant Kingdom ◽  
Ostreococcus Tauri

Abstract Background The tRNAs act as a bridge between the coding mRNA and incoming amino acids during protein translation. The anti-codon of tRNA recognizes the codon of the mRNA and deliver the amino acid into the protein translation chain. However, we did not know about the exact abundance of anti-codons in the genome and whether the frequency of abundance remains same across the plant lineage or not. Results Therefore, we analysed the tRNAnome of 128 species and reported an anti-codon table of the plant kingdom. We found that CAU anti-codon of tRNAMet has highest (5.039%) whereas CGC anti-codon of tRNAArg has lowest (0.004%) abundance. However, when we compared the anti-codon frequencies according to the tRNA isotypes, we found tRNALeu (7.808%) has highest abundance followed by tRNASer (7.668%) and tRNAGly (7.523%). Similarly, suppressor tRNA (0.036%) has lowest abundance followed by tRNASec (0.066%) and tRNAHis (2.109). The genome of Ipomoea nil, Papaver somniferum, and Zea mays encoded the highest number of anti-codons at 59 each whereas the genome of Ostreococcus tauri was found to encode only 18 isoacceptors. The tRNASec genes undergone losses more frequently than duplication and it has undergone anti-codon switch during the course of evolution. Conclusion The anti-codon table of the plant tRNA will enable us to understand the synonymous codon usage of the plant kingdom and can be very helpful to understand which codon is preferred over other during the translation.

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.

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