Sandbox Reserved 1759
From Proteopedia
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The protein of interest is the enzyme mevalonate 3,5-bisphosphate decarboxylase (MBD). The MBD enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction. | The protein of interest is the enzyme mevalonate 3,5-bisphosphate decarboxylase (MBD). The MBD enzyme was observed in Thermoplasma-type MVA pathway, specifically as a catalytic enzyme in the MBD reaction. The function of MBD is to catalyze the removal of the phosphate group from the 3rd carbon of mevalonate 3,5-bisphosphate (MVA3,5BP). The enzyme also accompanies the decarboxylation of the substrate. MBD acts upon MVA3,5BP to produce isopentnyl phosphate (IP), PO4, and CO2 in the MBD reaction. | ||
| - | <scene name='93/934003/Protein_view_2/1'>Ligand of interest</scene>, Oleic Acid (<scene name='93/934003/Ola/1'>OLA</scene>) | ||
== Biological relevance and broader implications == | == Biological relevance and broader implications == | ||
== Important amino acids== | == Important amino acids== | ||
| - | The <scene name='93/934003/Protein_view_2/1'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene> | + | The <scene name='93/934003/Protein_view_2/1'>ligand of interest</scene> in the MBD enzyme is called <scene name='93/934003/Ola/1'>Oleic acid (OLA)</scene> and is located within subunit A. OLA is hydrogen bonded to <scene name='93/934003/Arg128_bonded_to_ola/1'>Arg128</scene>. |
== Structural highlights == | == Structural highlights == | ||
| - | The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains with what appears to be a 60% alpha helixes (pink) and 40% beta sheets (yellow) when viewing the <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The two subunits are homodimers, containing 9 alpha helix and 15 beta sheets each. The alpha helixes and beta sheets loop and fold to form a <scene name='93/934003/Tertiary_structure/1'>3D globular protein</scene>. The <scene name='93/934003/Space_filling/1'>space filling</scene> model helps to highlight the globular nature of the protein. Amphipathic..... | + | The Protein is composed of alpha helix, beta sheet, and other structures. The protein consists of two major domains with what appears to be a 60% alpha helixes (pink) and 40% beta sheets (yellow) when viewing the <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The two subunits are homodimers, containing 9 alpha helix and 15 beta sheets each. The alpha helixes and beta sheets loop and fold to form a <scene name='93/934003/Tertiary_structure/1'>3D globular protein</scene>. The <scene name='93/934003/Space_filling/1'>space filling</scene> model helps to highlight the globular nature of the protein. Amphipathic.....In addition to the hydrogen bonding between OLA and Arg128, OLA is also hydrogen bonded to a water molecule which is hydrogen bonded to Arg128 as well |
</StructureSection> | </StructureSection> | ||
Revision as of 00:52, 12 December 2022
Mevalonate 3,5-Bisphosphate Decarboxylase Structure
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References
- ↑ Azami Y, Hattori A, Nishimura H, Kawaide H, Yoshimura T, Hemmi H. (R)-mevalonate 3-phosphate is an intermediate of the mevalonate pathway in Thermoplasma acidophilum. J Biol Chem. 2014 Jun 6;289(23):15957-67. doi: 10.1074/jbc.M114.562686. Epub 2014, Apr 22. PMID:24755225 doi:http://dx.doi.org/10.1074/jbc.M114.562686
