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| | <StructureSection load='4wxb' size='340' side='right'caption='[[4wxb]], [[Resolution|resolution]] 2.05Å' scene=''> | | <StructureSection load='4wxb' size='340' side='right'caption='[[4wxb]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4wxb]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Strt1 Strt1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WXB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WXB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4wxb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_thermophilus_CNRZ1066 Streptococcus thermophilus CNRZ1066]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WXB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glyA, str0755 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=299768 STRT1])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4wxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxb OCA], [https://pdbe.org/4wxb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wxb RCSB], [https://www.ebi.ac.uk/pdbsum/4wxb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wxb ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycine_hydroxymethyltransferase Glycine hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4wxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxb OCA], [http://pdbe.org/4wxb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wxb RCSB], [http://www.ebi.ac.uk/pdbsum/4wxb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wxb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GLYA_STRT1 GLYA_STRT1]] Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | + | [https://www.uniprot.org/uniprot/GLYA_STRT1 GLYA_STRT1] Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Serine hydroxymethyltransferase|Serine hydroxymethyltransferase]] | + | *[[Serine hydroxymethyltransferase 3D structures|Serine hydroxymethyltransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Glycine hydroxymethyltransferase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Strt1]] | + | [[Category: Streptococcus thermophilus CNRZ1066]] |
| - | [[Category: Bujons, J]] | + | [[Category: Bujons J]] |
| - | [[Category: Clapes, P]] | + | [[Category: Clapes P]] |
| - | [[Category: Hernandez, K]] | + | [[Category: Hernandez K]] |
| - | [[Category: Joglar, J]] | + | [[Category: Joglar J]] |
| - | [[Category: Parella, T]] | + | [[Category: Parella T]] |
| - | [[Category: Petrillo, G]] | + | [[Category: Petrillo G]] |
| - | [[Category: Uson, I]] | + | [[Category: Uson I]] |
| - | [[Category: Wandtke, C]] | + | [[Category: Wandtke C]] |
| - | [[Category: Zelen, I]] | + | [[Category: Zelen I]] |
| - | [[Category: Aldehyde]]
| + | |
| - | [[Category: Aldolase]]
| + | |
| - | [[Category: Catalysis]]
| + | |
| - | [[Category: Catalytic domain]]
| + | |
| - | [[Category: Chemical]]
| + | |
| - | [[Category: Escherichia coli]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Protein conformation]]
| + | |
| - | [[Category: Protein structure]]
| + | |
| - | [[Category: Serine hydrodymethyltransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
GLYA_STRT1 Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Publication Abstract from PubMed
alpha,alpha-Disubstituted alpha-amino acids are central to biotechnological and biomedical chemical processes for their own sake and as substructures of biologically active molecules for diverse biomedical applications. Structurally, these compounds contain a quaternary stereocenter, which is particularly challenging for stereoselective synthesis. The pyridoxal-5'-phosphate (PLP)-dependent L-serine hydroxymethyltransferase from Streptococcus thermophilus (SHMTSth ; EC 2.1.2.1) was engineered to achieve the stereoselective synthesis of a broad structural variety of alpha,alpha-dialkyl-alpha-amino acids. This was accomplished by the formation of quaternary stereocenters through aldol addition of the amino acids D-Ala and D-Ser to a wide acceptor scope catalyzed by the minimalist SHMTSth Y55T variant overcoming the limitation of the native enzyme for Gly. The SHMTSth Y55T variant tolerates aromatic and aliphatic aldehydes as well as hydroxy- and nitrogen-containing aldehydes as acceptors.
Engineered L-Serine Hydroxymethyltransferase from Streptococcus thermophilus for the Synthesis of alpha,alpha-Dialkyl-alpha-Amino Acids.,Hernandez K, Zelen I, Petrillo G, Uson I, Wandtke CM, Bujons J, Joglar J, Parella T, Clapes P Angew Chem Int Ed Engl. 2015 Jan 21. doi: 10.1002/anie.201411484. PMID:25611820[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hernandez K, Zelen I, Petrillo G, Uson I, Wandtke CM, Bujons J, Joglar J, Parella T, Clapes P. Engineered L-Serine Hydroxymethyltransferase from Streptococcus thermophilus for the Synthesis of alpha,alpha-Dialkyl-alpha-Amino Acids. Angew Chem Int Ed Engl. 2015 Jan 21. doi: 10.1002/anie.201411484. PMID:25611820 doi:http://dx.doi.org/10.1002/anie.201411484
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