Sandbox Reserved 1671
From Proteopedia
(Difference between revisions)
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The octantal was the best substrate with the lowest Km and the highest affinity out of all 23 substrates. | The octantal was the best substrate with the lowest Km and the highest affinity out of all 23 substrates. | ||
- | Ald-C is also a homodimer. The central beta sheets are surrounded by alpha helices to form the NAD(H) binding site. The C terminal region has a mixture of both alpha and betta domain, which includes the catalytic cysteine residue and forms the aldehyde – binding site.Due to the mutated cystine to an alanine there may have been a disturbance in a potential disulfides bridge that happens between 2 cysteines and are essential for stability.In this space fill scene you can see where the hydrogen bonds are. For the <scene name='87/873233/Backbone/1'>secondary structure</scene> of Ald-C the alpha helices and beta sheets are shown | + | Ald-C is also a homodimer. The central beta sheets are surrounded by alpha helices to form the NAD(H) binding site. The C terminal region has a mixture of both alpha and betta domain, which includes the catalytic cysteine residue and forms the aldehyde – binding site.Due to the mutated cystine to an alanine there may have been a disturbance in a potential disulfides bridge that happens between 2 cysteines and are essential for stability (<scene name='87/873233/Cys/1'>152,177</scene>). In this space fill scene you can see where the hydrogen bonds are. For the <scene name='87/873233/Backbone/1'>secondary structure</scene> of Ald-C the alpha helices and beta sheets are shown |
== Other important features == | == Other important features == | ||
Alanine substitutions of Glu 257 and Glu 391 severely disrupted AldC activity, showing that alanine had serious effects on other amino acids found along Ald-C. | Alanine substitutions of Glu 257 and Glu 391 severely disrupted AldC activity, showing that alanine had serious effects on other amino acids found along Ald-C. | ||
- | + | ||
</StructureSection> | </StructureSection> |
Revision as of 03:49, 19 April 2021
This Sandbox is Reserved from 01/25/2021 through 04/30/2021 for use in Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1665 through Sandbox Reserved 1682. |
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Ald-C
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References
Lee, S. G., Harline, K., Abar, O., Akadri, S. O., Bastian, A. G., Chen, H. S., Duan, M., Focht, C. M., Groziak, A. R., Kao, J., Kottapalli, J. S., Leong, M. C., Lin, J. J., Liu, R., Luo, J. E., Meyer, C. M., Mo, A. F., Pahng, S. H., Penna, V., Raciti, C. D., … Jez, J. M. (2020). The plant pathogen enzyme AldC is a long-chain aliphatic aldehyde dehydrogenase. The Journal of biological chemistry, 295(40), 13914–13926. https://doi.org/10.1074/jbc.RA120.014747 IAA (Indole-3-Acetic acid). (n.d.). Retrieved April 19, 2021, from https://www.goldbio.com/product/1311/iaa-indole-3-acetic-acid
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644