Summary
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1.
The “biosynthetic” l-threonine (deaminating) dehydratase o-7 marine planktonic species from 5 classes of algae showed several degrees of activation from monovalent inorganic cations. The activation was generally the strongest (3 to 5-fold) with K+ and NH4 +, and the weakest (1 to 2-fold) with Na+ and Tl+, whilst Li+, Rb+ and Cs+ showed intermediate orders varying with algal species. One blue-green alga was exceptional in showing strongest stimulation (5-fold) from Li+ and more pronounced activation from Na+ than Cs+ whilst a green alga showed another type of response with the least effect from Li+ and markedly greater activation from Rb+ than NH4 +.
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2.
The cation activation showed (i) “hyperbolic” kinetic response to ion concentration, and (ii) high specificity for monovalent inorganic cations, with indications of a coenzyme type of role for the alkalimetal type of ions.
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3.
Organic cations were inert and the divalent cations Mg2+, Ca2+, Zn2+, Cu2+ were either inhibitory or without effect.
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4.
Among the anions tested, chloride, bromide, fluoride, bicarbonate showed no effect, iodide, nitrate, chlorate were inhibitory, whilst phosphate and sulfate were slightly stimulatory.
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5.
It was concluded that the algal enzymes may have an absolute K+ or NH4 + requirement for in vivo expression of activity.
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Abbreviations
- TrixxH+ :
-
protonated tris(hydroxymethyl)methyl-amine
- Tricine:
-
N-tris(hydroxymethyl)methyl glycine
- Hepes:
-
N-2-hydroxyethylpiperazine-N′-2-ethane sulfonic acid
- Map:
-
2-methyl-2-amino-1-propanol
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Antia, N.J., Kripps, R.S. & Desai, I.D. l-Threonine deaminase in marine planktonic algae. Archiv. Mikrobiol. 85, 341–354 (1972). https://doi.org/10.1007/BF00549272
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DOI: https://doi.org/10.1007/BF00549272