Sandbox GGC4
From Proteopedia
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== Relevance == | == Relevance == | ||
| + | Lipoic Acid Is a prosthetic group for many dehydrogenase in ''E. coli'', and it is also needed for enzymes involved in the glycine cleavage system. A key example of use of lipoic acid is the E2 subunit of the pyruvate dehydrogenase complex. Lipoate attaches to a lysine on this subunit, and the sulfur on the ring of lipoic acid binds covalnetly with the incoming pyruvate to "shuttle" it to the SCoA complex for later use in the citric acid cycle. Lipoate protein Ligase A is the enzyme in ''e.Coli'' that attaches lipoate to the enzymes that need it. Humans Have a homolog to this enzyme, called lipoyltransferase, and the two enzymes share between 31%-35% identityWith each other. In contrast to the lipoate protein Ligase A, however, lipoyltransferase in humans is unable to catalyze the first part of the reaction in which an AMP is added to a lipoic acid. | ||
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| + | Research has found that lipoate protein Ligase A proteins are present in fairly small numbers in an ''e.coli'' cell (less than 10 per cell). Studies conducted on purified Lipoate protein Ligase found that the enzyme additionally requires Magnesium ions to functions properly, as well as lipoic acid and ATP. Lipoate protein Ligase can use both the R and S enantiomers of Lipoate as substrates, though it has a higher affinity for (R)-Lipoate. in addition to the enantiomers, other molecules similar in structure to lipoate, such as ocatnoate, can be incoporated into the enzymes active site, although with less affinity. | ||
== Structural highlights == | == Structural highlights == | ||
Revision as of 14:50, 20 April 2018
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This is a default text for your page Sandbox GGC4. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Contents |
Function
Lipoate Protein Ligase A is a monomeric protein in e. coli catalyzes the reaction to add lipoic acid to other enzymes that require it. This is a two step reaction. First, ATP is cleaved into AMP and pyrophosphate, and AMP is then attached to lipoate molecule. Then, Lipoate Protein Ligase attaches the lipoic acid to a desired protein; the AMP is removed from lipoate in the process. The lipoate is typically taken up by specific lysine residues in the receiving protein, and used as a prosthetic group.
Disease
Relevance
Lipoic Acid Is a prosthetic group for many dehydrogenase in E. coli, and it is also needed for enzymes involved in the glycine cleavage system. A key example of use of lipoic acid is the E2 subunit of the pyruvate dehydrogenase complex. Lipoate attaches to a lysine on this subunit, and the sulfur on the ring of lipoic acid binds covalnetly with the incoming pyruvate to "shuttle" it to the SCoA complex for later use in the citric acid cycle. Lipoate protein Ligase A is the enzyme in e.Coli that attaches lipoate to the enzymes that need it. Humans Have a homolog to this enzyme, called lipoyltransferase, and the two enzymes share between 31%-35% identityWith each other. In contrast to the lipoate protein Ligase A, however, lipoyltransferase in humans is unable to catalyze the first part of the reaction in which an AMP is added to a lipoic acid.
Research has found that lipoate protein Ligase A proteins are present in fairly small numbers in an e.coli cell (less than 10 per cell). Studies conducted on purified Lipoate protein Ligase found that the enzyme additionally requires Magnesium ions to functions properly, as well as lipoic acid and ATP. Lipoate protein Ligase can use both the R and S enantiomers of Lipoate as substrates, though it has a higher affinity for (R)-Lipoate. in addition to the enantiomers, other molecules similar in structure to lipoate, such as ocatnoate, can be incoporated into the enzymes active site, although with less affinity.
Structural highlights
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</StructureSection>
References
- ↑ 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
