Serine acetyltransferase
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | The structure of the complex of SAT with its substrate serine suggest that His169 and Asp154 form a catalytic dyad and that His189 may stabilize the oxyanion intermediate. | + | The structure of the complex of SAT with its substrate serine suggest that <scene name='80/801782/Cv/3'>His169 and Asp154 form a catalytic dyad</scene> and that <scene name='80/801782/Cv/4'>His189 may stabilize the oxyanion intermediate</scene>. <scene name='80/801782/Cv/7'>Glu177 helps to position Arg203 and His204</scene> for <scene name='80/801782/Cv/6'>TextToBeDisplayed</scene>serine binding</scene> (water molecules shown as red spheres). Arg253 is important for the catalytic efficiency of SAT. Lys230 is required for the cofactor acetyl-CoA binding<ref>PMID:24225955</ref>. |
</StructureSection> | </StructureSection> | ||
Revision as of 12:43, 3 December 2018
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3D structures of serine acetyltransferase
Updated on 03-December-2018
References
- ↑ Gerlt JA, Babbitt PC, Rayment I. Divergent evolution in the enolase superfamily: the interplay of mechanism and specificity. Arch Biochem Biophys. 2005 Jan 1;433(1):59-70. doi: 10.1016/j.abb.2004.07.034. PMID:15581566 doi:http://dx.doi.org/10.1016/j.abb.2004.07.034
- ↑ Yi H, Dey S, Kumaran S, Lee SG, Krishnan HB, Jez JM. Structure of Soybean Serine Acetyltransferase and Formation of the Cysteine Regulatory Complex as a Molecular Chaperone. J Biol Chem. 2013 Nov 13. PMID:24225955 doi:http://dx.doi.org/10.1074/jbc.M113.527143
