Serine hydroxymethyltransferase. 31P nuclear magnetic resonance study of the enzyme-bound pyridoxal 5'-phosphate.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference25 articles.
1. The interconversion of serine and glycine: participation of pyridoxal phosphate
2. Molecular weight and subunits of serine transhydroxymethylase
3. Serine Transhydroxymethylase
4. Reaction of apoaspartate aminotransferase with analogs of pyridoxal phosphate
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2. Specificity of Gβγ Signaling to Kir3 Channels Depends on the Helical Domain of Pertussis Toxin-sensitive Gα Subunits;Journal of Biological Chemistry;2007-11
3. The N Terminus of GTPγS-activated Transducin α-Subunit Interacts with the C Terminus of the cGMP Phosphodiesterase γ-Subunit;Journal of Biological Chemistry;2006-03
4. Ionization state of pyridoxal 5′-phosphate in d-serine dehydratase, dialkylglycine decarboxylase and tyrosine phenol-lyase and the influence of monovalent cations as inferred by 31P NMR spectroscopy;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2006-02
5. Serine Hydroxymethyltransferase: Role of Glu75 and Evidence that Serine Is Cleaved by a Retroaldol Mechanism;Biochemistry;2004-05-11
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