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KMID : 0364820190550010009
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Korean Journal of Microbiology
2019 Volume.55 No. 1 p.9 ~ p.16
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Crystal structure of α-acetolactate decarboxylase from Bacillus subtilis subspecies spizizenii
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Eom Ji-Young
Oh Han-Byeol
Yoon Sung-Il
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Abstract
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Acetoin is generated by numerous microorganisms using α-acetolactate decarboxylase (ALDC) to prevent overacidificationof cells and their environment and to store remaining energy. Because acetoin has been used as a safe flavor enhancer in foodproducts, industries have been interested in biotechnologicalproduction of acetoin using ALDC. ALDC is a metal-dependentenzyme that produces acetoin from α-acetolactate throughdecarboxylation reaction. Here, we report the crystal structureof ALDC from Bacillus subtilis subspecies spizizenii (bssALDC)at 1.7 A resolution. bssALDC folds into a two-domain α/βstructure where two β-sheets form a central core. bssALDCassembles into a dimer through central hydrophobic interactionsand peripheral hydrophilic interactions. bssALDC coordinatesa zinc ion using three histidine residues and three watermolecules. Based on comparative analyses of ALDC structuresand sequences, we propose that the active site of bssALDCincludes the zinc ion and its neighboring bssALDC residues.
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KEYWORD
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Bacillus subtilis, acetoin, α-acetolactate decarboxylase, structure, zinc
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