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Carbohydrates Stimulate Ethylene Production in Tobacco Leaf Discs : III. Stimulation of Enzymic Hydrolysis of Indole-3-Acetyl-l-Alanine.
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The sucrose-stimulated in vivo hydrolysis of indole-3-acetyl-l-alanine (IAAIa) in tobacco (Nicotiana tabacum L.) leaf discs was confirmed by in vitro analysis of an IAAIa-hydrolyzing enzyme isolated from the same tissue. The enzymic activity could be stimulated by either aging of the tissue or by
The Arabidopsis thaliana isogene NIT4 and its orthologs in tobacco encode beta-cyano-L-alanine hydratase/nitrilase.
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Nitrilases (nitrile aminohydrolases, EC ) are enzymes that catalyze the hydrolysis of nitriles to the corresponding carbon acids. Among the four known nitrilases of Arabidopsis thaliana, the isoform NIT4 is the most divergent one, and homologs of NIT4 are also known from species not belonging to the
Biological activities of indoleacetylamino acids and their use as auxins in tissue culture.
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THE AUXIN ACTIVITIES OF A NUMBER OF INDOLEACETYLAMINO ACID CONJUGATES HAVE BEEN DETERMINED IN THREE TEST SYSTEMS: growth of tomato hypocotyl explants (Lycopersicon esculentum Mill. cv. Marglobe); growth of tobacco callus cultures (Nicotiana tabacum L. cv. Wisconsin 38); and ethylene production from
Relative toxicities and neuromuscular nicotinic receptor agonistic potencies of anabasine enantiomers and anabaseine.
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Anabasine occurring in wild tree tobacco (Nicotiana glauca) and anabaseine occurring in certain animal venoms are nicotinic receptor agonist toxins. Anabasine lacks the imine double bond of anabaseine; the two possible enantiomers of anabasine occur in N. glauca. A comparision of the relative
Carbohydrates stimulate ethylene production in tobacco leaf discs : I. Interaction with auxin and the relation to auxin metabolism.
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Various naturally occurring carbohydrates, applied at a concentration range of 1 to 100 mm, stimulated ethylene production for several days in indoleacetic acid (IAA)-treated or untreated tobacco (Nicotiana tabacum L. cv ;Xanthi') leaf discs. The lag period for this sugar-stimulated ethylene
Cyanide metabolism in higher plants: cyanoalanine hydratase is a NIT4 homolog.
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Cyanoalanine hydratase (E.C. 4.2.1.65) is an enzyme involved in the cyanide detoxification pathway of higher plants and catalyzes the hydrolysis of beta-cyano-L-alanine to asparagine. We have isolated the enzyme from seedlings of blue lupine (Lupinus angustifolius) to obtain protein sequence
Antimicrobial activity of bacteriophage derived triple fusion protein against Staphylococcus aureus.
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The increasing spread of antibiotic-resistant microorganisms has led to the necessity of developing alternative antimicrobial treatments. The use of peptidoglycan hydrolases is a promising approach to combat bacterial infections. In our study, we constructed a 2 kb-triple-acting fusion gene
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