Producción científica por año
Producción científica por año
Descripción
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.05
Classification:TRANSFERASE
Release Date:2015-02-04
Deposition Date:2014-11-13
Revision Date:2015-03-04#2017-09-13
Molecular Weight:187927.97
Macromolecule Type:Protein
Residue Count:1712
Atom Site Count:12469
DOI:10.2210/pdb4wxb/pdb
Abstract:
α,α-Disubstituted α-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 (SHMT(Sth); EC 2.1.2.1) was engineered to achieve the stereoselective synthesis of a broad structural variety of α,α-dialkyl-α-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 SHMT(Sth) Y55T variant overcoming the limitation of the native enzyme for Gly. The SHMT(Sth) Y55T variant tolerates aromatic and aliphatic aldehydes as well as hydroxy- and nitrogen-containing aldehydes as acceptors.
Resolution:2.05
Classification:TRANSFERASE
Release Date:2015-02-04
Deposition Date:2014-11-13
Revision Date:2015-03-04#2017-09-13
Molecular Weight:187927.97
Macromolecule Type:Protein
Residue Count:1712
Atom Site Count:12469
DOI:10.2210/pdb4wxb/pdb
Abstract:
α,α-Disubstituted α-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 (SHMT(Sth); EC 2.1.2.1) was engineered to achieve the stereoselective synthesis of a broad structural variety of α,α-dialkyl-α-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 SHMT(Sth) Y55T variant overcoming the limitation of the native enzyme for Gly. The SHMT(Sth) Y55T variant tolerates aromatic and aliphatic aldehydes as well as hydroxy- and nitrogen-containing aldehydes as acceptors.
| Datos disponibles | 4 feb 2015 |
|---|---|
| Editor | RCSB-PDB |
Producción científica
- 1 Artículo
-
Engineered L-serine hydroxymethyltransferase from streptococcus thermophilus for the synthesis of α,α-dialkyl-α-amino acids
Hernandez, K., Zelen, I., Petrillo, G., Usón, I., Wandtke, C. M., Bujons, J., Joglar, J., Parella, T. & Clapés, P., 2 mar 2015, En: Angewandte Chemie - International Edition. 54, 10, p. 3013-3017Producción científica: Contribución a una revista › Artículo › Investigación › revisión exhaustiva
39 Citas (Scopus)
Conjuntos de datos
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4WXG : Crystal structure of L-Serine Hydroxymethyltransferase in complex with a mixture of L-allo-Threonine and Glycine
Hernandez, K. (Creador), Zelen, I. (Colaborador), Petrillo, G. (Colaborador), Usón, I. (Colaborador), Wandtke, C. M. (Colaborador), Bujons, J. (Colaborador), Joglar, J. (Colaborador), Parella, T. (Colaborador) & Clapés, P. (Colaborador), RCSB-PDB, 4 feb 2015
DOI: 10.2210/pdb4wxg/pdb, https://www.rcsb.org/structure/4WXG
Dataset: Conjunto de datos
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4WXF : Crystal structure of L-Serine Hydroxymethyltransferase in complex with glycine
Hernandez, K. (Creador), Zelen, I. (Colaborador), Petrillo, G. (Colaborador), Usón, I. (Colaborador), Bujons, J. (Colaborador), Joglar, J. (Colaborador), Parella, T. (Colaborador) & Clapés, P. (Colaborador), RCSB-PDB, 4 feb 2015
DOI: 10.2210/pdb4wxf/pdb, https://www.rcsb.org/structure/4WXF
Dataset: Conjunto de datos