Sandbox Reserved 1808

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== Function of Lactonase Enzyme ==
== Function of Lactonase Enzyme ==
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The organism from which this protein is found is Rhodopsuedomonas plaustris (Rpa3624). The basic function for the lactonase enzyme is to break down valerolactone.
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The organism from which this protein is found is Rhodopsuedomonas plaustris (Rpa3624). The basic function for the lactonase enzyme is to break down valerolactone. Naturally occurring lactones function as metabolic intermediates, signaling molecules, antibiotics, and more.
== Biological Relevance and Broader Implications ==
== Biological Relevance and Broader Implications ==
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Lactones are a diverse set of cyclic ester-containing compounds that play many roles in chemical and biological systems. Naturally occurring lactones function as metabolic intermediates, signaling molecules, antibiotics, and more. GVL is one such lactone used as a solvent that can be both produced from plant biomass and used to dissolve plant cell walls into sugars and aromatic molecules for subsequent microbial conversion to fuels and chemicals. Even after the majority is removed from the dissolved biomass, the residual GVL can be toxic to microbial fermentation. Residual GVL could also represent a significant carbon and energy source for tolerant microbes that could assimilate this lactone or convert it into other valuable products. The use of GVL as a renewable solvent for plant deconstruction would benefit from the identification of microbial enzymes that can hydrolyze the lactone ring of this compound.
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Lactones are a diverse set of cyclic ester-containing compounds that play many roles in chemical and biological systems. GVL is one such lactone used as a solvent that can be both produced from plant biomass and used to dissolve plant cell walls into sugars and aromatic molecules for subsequent microbial conversion to fuels and chemicals. Even after the majority is removed from the dissolved biomass, the residual GVL can be toxic to microbial fermentation. Residual GVL could also represent a significant carbon and energy source for tolerant microbes that could assimilate this lactone or convert it into other valuable products. The use of GVL as a renewable solvent for plant deconstruction would benefit from the identification of microbial enzymes that can hydrolyze the lactone ring of this compound.
== Important Amino Acids==
== Important Amino Acids==
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The first five amino acids of the amino terminus at physiological pH are MSNVR.
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The first five amino acids of the amino terminus at physiological pH are MSNVR. The catalytic amino acids are located in the active center and are responsible for accelerating the enzyme-catalyzed reaction. The catalytic amino acids are N123, N172, and S230.
== Structural Highlights ==
== Structural Highlights ==
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Secondary Structure: Consists of six blades of B-propeller, phosphate molecule bound to calcium and sodium ion with a helix attached to it.
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This is a <scene name='95/954105/Test/1'>test image</scene>.
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Tertiary Structure: Calcium coordination sphere shows the contacts holding the calcium ion in place.
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Quaternary structure: Carbonyl oxygen of 2-HQ overlaps with one of the phosphate oxygens.
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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</StructureSection>
</StructureSection>
== References ==
== References ==
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<references/>
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<Bingman, C.A., Hall, B.W., Smith, R.W., Fox, B.G., Donohue, T.J. (2022).© 2022 THE AUTHORS. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.DOI: https://doi.org/10.1016/j.jbc.2022.102782
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Current revision

This Sandbox is Reserved from Mar 1 through Jun 1, 2023 for use in the course CHEM 351 Biochemistry taught by Bonnie_Hall at the Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1796 through Sandbox Reserved 1811.
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Lactonase Enzyme Structure

Caption for this structure

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References

<Bingman, C.A., Hall, B.W., Smith, R.W., Fox, B.G., Donohue, T.J. (2022).© 2022 THE AUTHORS. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.DOI: https://doi.org/10.1016/j.jbc.2022.102782

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