Structure-Based Mechanism for Early PLP-Mediated Steps of Rabbit Cytosolic Serine Hydroxymethyltransferase Reaction

Serine hydroxymethyltransferase catalyzes the reversible interconversion of L-serine and glycine with transfer of one-carbon groups to and from tetrahydrofolate. Active site residue Thr254 is known to be involved in the transaldimination reaction, a crucial step in the catalytic mechanism of all pyr...

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Veröffentlicht in:	BioMed research international 2013-01, Vol.2013 (2013), p.1-13
Hauptverfasser:	Schirch, Verne, Wright, H. Tonie, di Salvo, Martino Luigi, Scarsdale, J. Neel, Kazanina, Galina, Contestabile, Roberto
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino acids Animals Binding Sites Biology Biomedical research Catalysis Catalytic Domain - genetics Crystallography, X-Ray Crystals Enzymes Gene Expression Glycine Hydroxymethyltransferase - chemistry Glycine Hydroxymethyltransferase - metabolism Hydrogen Bonding Kinetics Mutagenesis, Site-Directed Mutation Physiological aspects Potassium Pyridoxal Phosphate - chemistry Pyridoxal Phosphate - metabolism Rabbits Serine Structure-Activity Relationship Studies Transferases
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