The heme moiety in peanut peroxidase

1984 ◽  
Vol 62 (11) ◽  
pp. 1046-1050 ◽  
Author(s):  
R. N. Chibbar ◽  
R. Cella ◽  
R. B. Van Huystee
Keyword(s):  
Peroxidase Activity ◽  
Active Site ◽  
Oxidase Activity ◽  
Indoleacetic Acid ◽  
Iaa Oxidase ◽  
Equimolar Ratio ◽  
Immunological Properties ◽  
Peanut Peroxidase

Heme is present in an equimolar ratio to the apoprotein in the major cationic fraction of peanut peroxidase. The removal of heme from the holoenzyme does not affect the physicochemical and immunological properties of the apoperoxidase, however peroxidase activity is completely lost. The indoleacetic acid (IAA) oxidase activity of the apoperoxidase is reduced to 1/20 of the original holoenzyme. Both the peroxidase and IAA-oxidase activity could partially be restored in the holoenzyme reconstituted with hemin. It is suggested that heme may also participate in the IAA-oxidase activity possibly by altering the active site.

The regulation of peroxidase activity by gibberellin and auxin in pea stem segments

1973 ◽  
Vol 51 (11) ◽  
pp. 2237-2242 ◽  
Author(s):  
Ralph Ockerse ◽  
Laura M. Mumford
Keyword(s):  
Peroxidase Activity ◽  
Oxidase Activity ◽  
Actinomycin D ◽  
Indoleacetic Acid ◽  
Growth Media ◽  
Slight Reduction ◽  
Iaa Oxidase ◽  
Pisum Sativum L ◽  
Reduced Activity ◽  
Stem Segments

Peroxidase activity in excised stem segments of Pisum sativum L. cv. Progress No. 9 increases linearly during incubation in buffered medium. Gibberellic acid (GA) causes a slight reduction in activity whereas indoleacetic acid (IAA) treatment completely prevents this rise. Excision produces two new cathodic isoperoxidases near the cut ends. Their appearance is prevented by cycloheximide, actinomycin D, and IAA; G A enhances this IAA-induced repression. GA alone stimulates one of the isozymes but does not affect the other one. Peroxidase leakage is stimulated by GA and inhibited by IAA treatment. The activity is entirely confined to the isoperoxidases produced in response to injury.IAA oxidase activity in incubated segments was slightly elevated over that of freshly cut ones. However, differences in activity among hormone treatments were small. IAA oxidase was also demonstrated in growth media and only IAA treatment reduced activity. Both peroxidases in the medium were isolated by column chromatography. Surprisingly, the purified isozymes appear to be essentially devoid of IAA oxidase activity.

scholarly journals Preliminary characterization of peroxidase isozymes isolated from two flax genotrophs

1977 ◽  
Vol 55 (11) ◽  
pp. 1465-1473 ◽  
Author(s):  
M. A. Fieldes ◽  
C. L. Deal ◽  
H. Tyson
Keyword(s):  
Molecular Weight ◽  
Oxidase Activity ◽  
Indoleacetic Acid ◽  
Relative Mobility ◽  
Fresh Weight ◽  
Iaa Oxidase ◽  
Peroxidase Isozymes ◽  
Flax Genotrophs ◽  
Very High

Four peroxidase (EC 1.11.1.7) isozymes were isolated from each of two flax genotrophs. All four isozymes were glycoproteins and all exhibited indoleacetic acid (IAA) oxidase activity. The percentage purity of two of the isozymes was very high; these isozymes differed in percentage carbohydrate and in peroxidase and IAA oxidase specific activities. Three of the isozymes displayed molecular weight values of about 43 000; for the fourth, molecular weight was considerably higher. Corresponding isozymes from the genotrophs and from two other flax genotypes displayed molecular weight differences which corresponded to electrophoretic relative mobility differences. Enzyme yield per unit fresh weight was higher for one genotroph than the other, and the balance between peroxidase activity and IAA oxidase activity between the genotrophs was different.

An interrelationship among peroxidase, IAA oxidase, and polyphenol oxidase from peanut cells

1977 ◽  
Vol 55 (20) ◽  
pp. 2630-2635 ◽  
Author(s):  
O. P. Srivastava ◽  
R. B. van Huystee
Keyword(s):  
Acetic Acid ◽  
Polyphenol Oxidase ◽  
Peroxidase Activity ◽  
Active Site ◽  
Indole Acetic Acid ◽  
Phenol Oxidase ◽  
Iaa Oxidase

Two methods were used to separate heme and apoenzyme from the holoenzyme of peroxidase (EC 1.11.1.7) isolated from medium of cultured peanut cells. Apoenzyme prepared by either method lacked peroxidase activity but possessed indole acetic acid (IAA) oxidase and poly phenol oxidase (PPO) (EC 1.14.18.1) activity. When the holoenzyme was reconstituted with heme and apoenzyme, peroxidase activity was restored. The studies on the active site revealed that PPO and IAA oxidase share the same active site on the apoenzyme.

scholarly journals Direct Probing of Copper Active Site and Free Radical Formed during Bicarbonate-dependent Peroxidase Activity of Bovine and Human Copper,Zinc-superoxide Dismutases

2004 ◽  
Vol 279 (31) ◽  
pp. 32534-32540 ◽  
Author(s):  
Chandran Karunakaran ◽  
Hao Zhang ◽  
John P. Crow ◽  
William E. Antholine ◽  
B. Kalyanaraman
Keyword(s):  
Free Radical ◽  
Peroxidase Activity ◽  
Active Site ◽  
Superoxide Dismutases ◽  
Copper Zinc ◽  
Copper Zinc Superoxide Dismutases

Isolation and Characterization of Flavonol Converting Enzymes from Mentha piperita Plants and from Mentha arvensis Cell Suspension Cultures

1979 ◽  
Vol 34 (3-4) ◽  
pp. 200-209 ◽  
Author(s):  
Gudrun Frey-Schröder ◽  
Wolfgang Barz
Keyword(s):  
Cell Suspension ◽  
Oxidase Activity ◽  
Enzyme Reaction ◽  
Cell Suspension Cultures ◽  
Suspension Cultures ◽  
Mentha Piperita ◽  
Mentha Arvensis ◽  
Iaa Oxidase ◽  
Isolation And Characterization ◽  
Group I

Abstract Peroxidases from several plants, including horseradish peroxidase, were capable of converting flavonols to the corresponding 2,3-dihydroxyflavanones in presence of H2O2 . Contrastingly, protein extracts from Mentha piperita plants and Mentha arvensis cell suspension cultures perform ed the same enzymatic step in absence of H2O2 , but only with quercetin, not with kaempferol. H2O2-independent, quercetin converting enzymes were isolated and purified from these extracts, and they could be classified in two groups according to the extent of stimulation of the enzyme reaction by H2O2 . Enzymes from group I were stimulated by exogenous H2O2 , and they resembled horse­ radish peroxidase in several aspects. They possessed IAA oxidase activity, but quercetin was the preferred substrate. Enzymes from group II from the plants appeared to be a distinctly different set of enzymes. They were not stimulated by H2O2 , but required molecular oxygen and converted only 3,3′,4′-trihydroxyflavones under aerobic conditions. Also, they showed no Soret-bands and possessed no IAA oxidase activity. These proteins appear to be a new class of enzymes participating in the first step of flavonol degradation in plants.

Localisation structurale et ultrastructurale d'activités peroxydasiques dans les parois du mésophylle et des fibres en cours de lignification chez l'alfa (Stipa tenacissima)

1984 ◽  
Vol 62 (12) ◽  
pp. 2644-2649 ◽  
Author(s):  
M. Harche
Keyword(s):  
Peroxidase Activity ◽  
Oxidase Activity ◽  
Cell Walls ◽  
Secondary Wall ◽  
Outer Part ◽  
Potassium Cyanide ◽  
Primary Wall ◽  
Stipa Tenacissima ◽  
Parenchyma Cells

Using diaminobenzidine as substrate, peroxidase activity was localized in the walls of parenchyma cells and differentiating fibres. In mature fibres and parenchyma a slight activity could be recognized in primary walls only. In parenchyma cells, peroxidase activity was fairly inhibited with heat, potassium cyanide, and aminotriazole, which could indicate the presence of catalase within the cell walls. However, in plasmodesmatal regions peroxidases were- resistant to the above inhibitors. Syringaldazine oxidase activity was present only in the primary wall and the outer part of the secondary wall of differentiating fibres. The parallelism between lignification and peroxidase activity in the secondary walls supports the hypothesis of the involvement of these enzymes in the lignification process.

Indoleacetic Acid Oxidase Activity of Wheat Peroxidase*

1962 ◽  
Vol 52 (6) ◽  
pp. 444-451 ◽  
Author(s):  
MASATERU SHIN ◽  
WATARU NAKAMURA
Keyword(s):  
Oxidase Activity ◽  
Indoleacetic Acid ◽  
Acid Oxidase ◽  
Indoleacetic Acid Oxidase
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