The action of some enzymes on homolysine derivatives

1968 ◽  
Vol 46 (4) ◽  
pp. 387-389 ◽  
Author(s):  
John H. Seely ◽  
Leo Benoiton
Keyword(s):  
Amino Acid ◽  
Ethyl Ester ◽  
Enzyme Preparation ◽  
Acid Oxidase ◽  
Lysine Decarboxylase ◽  
Amino Acid Oxidase ◽  
Kidney Enzyme ◽  
Chicken Kidney ◽  
Hog Kidney

DL-Homolysine was resistant to the action of lysine decarboxylase from Bacterium cadaveris, but was oxidized by L-amino acid oxidase from Crotalus adamanteus. ε-N-Acetyl-DL-homolysine was not hydrolyzed by ε-lysine acylase from hog kidney, but was hydrolyzed by a chicken kidney enzyme preparation. Hog kidney acylase showed slight activity towards α-N,ζ-N-dichloroacetyl- and α-N-chloroacetyl-ζ-N-carbobenzoxy-DL-homolysine. DL-Homolysine ethyl ester was hydrolyzed by trypsin at a rate one-eighth of that for lysine ethyl ester.

Impairment of Platelet Aggregation by Echis colorata Venom Mediated by L-Amino Acid Oxidase or H2O2

1982 ◽  
Vol 48 (03) ◽  
pp. 277-282 ◽  
Author(s):  
I Nathan ◽  
A Dvilansky ◽  
T Yirmiyahu ◽  
M Aharon ◽  
A Livne
Keyword(s):  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Platelet Aggregation ◽  
Snake Venom ◽  
Oxidase Activity ◽  
Enzyme Preparation ◽  
Acid Oxidase ◽  
Crude Venom ◽  
Amino Acid Oxidase ◽  
Hemostatic Disorders

SummaryEchis colorata bites cause impairment of platelet aggregation and hemostatic disorders. The mechanism by which the snake venom inhibits platelet aggregation was studied. Upon fractionation, aggregation impairment activity and L-amino acid oxidase activity were similarly separated from the crude venom, unlike other venom enzymes. Preparations of L-amino acid oxidase from E.colorata and from Crotalus adamanteus replaced effectively the crude E.colorata venom in impairment of platelet aggregation. Furthermore, different treatments known to inhibit L-amino acid oxidase reduced in parallel the oxidase activity and the impairment potency of both the venom and the enzyme preparation. H2O2 mimicked characteristically the impairment effects of L-amino acid oxidase and the venom. Catalase completely abolished the impairment effects of the enzyme and the venom. It is concluded that hydrogen peroxide formed by the venom L-amino acid oxidase plays a role in affecting platelet aggregation and thus could contribute to the extended bleeding typical to persons bitten by E.colorata.

The Purification of Hog Kidney D-Amino Acid Oxidase

1956 ◽  
Vol 78 (7) ◽  
pp. 1363-1367 ◽  
Author(s):  
F. P. Veitch ◽  
Robert McComb
Keyword(s):  
Amino Acid ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Hog Kidney

scholarly journals The mechanism of action of serine transhydroxymethylase

1970 ◽  
Vol 116 (2) ◽  
pp. 277-286 ◽  
Author(s):  
P. M. Jordan ◽  
M. Akhtar
Keyword(s):  
Schiff Base ◽  
Amino Acid ◽  
Hydrogen Atom ◽  
Mechanism Of Action ◽  
Active Site ◽  
Enzyme Preparation ◽  
Pyridoxal Phosphate ◽  
Acid Oxidase ◽  
Amino Acid Oxidase

1. The preparation of stereospecifically tritiated glycines and the determination of their absolute configurations by the use of d-amino acid oxidase are described. 2. The reaction catalysed by serine transhydroxymethylase, which results in the conversion of glycine into serine, has been separated into at least four partial reactions. It is suggested that the first event in this conversion is the formation of a Schiff base intermediate of glycine and pyridoxal phosphate. The next important step involves the removal of the 2S-hydrogen atom of glycine to give a carbanion intermediate. Experiments pertinent to the mechanism of conversion of this carbanion intermediate into serine are described. 3. The enzyme preparation catalysing the conversion of glycine into serine also participates in the conversion of glycine into threonine and allothreonine. In both these conversions, glycine → serine and glycine → threonine, the 2S-hydrogen atom of glycine is eliminated and the 2R-hydrogen atom of glycine is retained. 4. In the light of these experiments the mechanism of action of serine transhydroxymethylase is discussed. It is suggested that methylenetetrahydrofolate is the carrier of formaldehyde, from which formaldehyde may be liberated at the active site of the enzyme, thus allowing the overall reaction to take place.

Association-Dissociation of the Flavoprotein Hog Kidney D-Amino Acid Oxidase

1977 ◽  
Vol 82 (5) ◽  
pp. 1247-1255 ◽  
Author(s):  
Kihachiro HORIIKE ◽  
Kiyoshi SHIGA ◽  
Yasuzo NISHINA ◽  
Akio ISOMOTO ◽  
Toshio YAMANO
Keyword(s):  
Amino Acid ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Hog Kidney

scholarly journals The L-Amino Acid Oxidase from Silkworm Eggs (Bombyx mori L.)

1963 ◽  
Vol 46 (5) ◽  
pp. 1087-1094 ◽  
Author(s):  
Sadao Kotaka
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Physicochemical Properties ◽  
Bombyx Mori ◽  
Enzyme Preparation ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Preparation Methods ◽  
Crude Preparation ◽  
Bombyx Mori L

An enzyme which catalyzes the oxidation of L-amino acids has been isolated from silkworm eggs (Bombyx mori L.), and purified. The activity of the enzyme preparation is about 1584 times more than that of the crude preparation. Methods of purification of the enzyme are described in detail and certain physicochemical properties of the enzyme are also described.

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