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Flexible Enantioselectivity of Tryptophanase Attributable to Benzene Ring in Heterocyclic Moiety of D-Tryptophan

Sustainable Environmental Studies, Graduate School of Life and Environmental Sciences, University of Tsukuba, Tsukuba, Ibaraki 305-8572, Japan
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Life 2012, 2(2), 215-228; https://doi.org/10.3390/life2020215
Received: 23 March 2012 / Revised: 2 May 2012 / Accepted: 17 May 2012 / Published: 30 May 2012
(This article belongs to the Special Issue Origin of Life - Feature Papers)
The invariance principle of enzyme enantioselectivity must be absolute because it is absolutely essential to the homochiral biological world. Most enzymes are strictly enantioselective, and tryptophanase is one of the enzymes with extreme absolute enantioselectivity for L-tryptophan. Contrary to conventional knowledge about the principle, tryptophanase becomes flexible to catalyze D-tryptophan in the presence of diammonium hydrogenphosphate. Since D-amino acids are ordinarily inert or function as inhibitors even though they are bound to the active site, the inhibition behavior of D-tryptophan and several inhibitors involved in this process was examined in terms of kinetics to explain the reason for this flexible enantioselectivity in the presence of diammonium hydrogenphosphate. Diammonium hydrogenphosphate gave tryptophanase a small conformational change so that D-tryptophan could work as a substrate. As opposed to other D-amino acids, D-tryptophan is a very bulky amino acid with a benzene ring in its heterocyclic moiety, and so we suggest that this structural feature makes the catalysis of D-tryptophan degradation possible, consequently leading to the flexible enantioselectivity. The present results not only help to understand the mechanism of enzyme enantioselectivity, but also shed light on the origin of homochirality. View Full-Text
Keywords: tryptophanase; D-tryptophan; flexible stereoselectivity; diammoniumhydrogen phosphate; origin of homochirality tryptophanase; D-tryptophan; flexible stereoselectivity; diammoniumhydrogen phosphate; origin of homochirality
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MDPI and ACS Style

Shimada, A.; Ozaki, H. Flexible Enantioselectivity of Tryptophanase Attributable to Benzene Ring in Heterocyclic Moiety of D-Tryptophan. Life 2012, 2, 215-228. https://doi.org/10.3390/life2020215

AMA Style

Shimada A, Ozaki H. Flexible Enantioselectivity of Tryptophanase Attributable to Benzene Ring in Heterocyclic Moiety of D-Tryptophan. Life. 2012; 2(2):215-228. https://doi.org/10.3390/life2020215

Chicago/Turabian Style

Shimada, Akihiko; Ozaki, Haruka. 2012. "Flexible Enantioselectivity of Tryptophanase Attributable to Benzene Ring in Heterocyclic Moiety of D-Tryptophan" Life 2, no. 2: 215-228. https://doi.org/10.3390/life2020215

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