Abstract
The 31P NMR spectroscopy of three pyridoxal 5′-phosphate- dependent enzymes, monomeric d-serine dehydratase, tetrameric dialkylglycine decarboxylase and tetrameric tyrosine phenol-lyase, whose enzymatic activities are dependent on alkali metal ions, was studied. 31P NMR spectra of the latter two enzymes have never been reported, their 3D-structures, however, are available. The cofactor phosphate chemical shift of all three enzymes changes by ∼3 ppm as a function of pH, indicating that the phosphate group changes from being monoanionic at low pH to dianionic at high pH. The 31P NMR signal of the phosphate group of pyridoxal 5′-phosphate provides a measure of the active site changes that occur when various alkali metal ions are bound. Structural information is used to assist in the interpretation of the chemical shift changes observed. For d-serine dehydratase, no structural data are available but nevertheless the metal ion arrangement in the PLP binding site can be predicted from 31P NMR data.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 230-238 |
| Number of pages | 9 |
| Journal | Biochimica et Biophysica Acta - Proteins and Proteomics |
| Volume | 1764 |
| Issue number | 2 |
| DOIs | |
| State | Published - Feb 2006 |
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Keywords
- 31P chemical shift
- D-serine dehydratase
- Dialkylglycine decarboxylase
- Monovalent cations
- Ppyridoxal 5′-phosphate
- Tyrosine phenol-lyase
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Genetics
Cite this
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. / Schnackerz, Klaus D.; Keller, John; Phillips, Robert S.; Toney, Michael D.
In: Biochimica et Biophysica Acta - Proteins and Proteomics, Vol. 1764, No. 2, 02.2006, p. 230-238.Research output: Contribution to journal › Article
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TY - JOUR
T1 - 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
AU - Schnackerz, Klaus D.
AU - Keller, John
AU - Phillips, Robert S.
AU - Toney, Michael D.
PY - 2006/2
Y1 - 2006/2
N2 - The 31P NMR spectroscopy of three pyridoxal 5′-phosphate- dependent enzymes, monomeric d-serine dehydratase, tetrameric dialkylglycine decarboxylase and tetrameric tyrosine phenol-lyase, whose enzymatic activities are dependent on alkali metal ions, was studied. 31P NMR spectra of the latter two enzymes have never been reported, their 3D-structures, however, are available. The cofactor phosphate chemical shift of all three enzymes changes by ∼3 ppm as a function of pH, indicating that the phosphate group changes from being monoanionic at low pH to dianionic at high pH. The 31P NMR signal of the phosphate group of pyridoxal 5′-phosphate provides a measure of the active site changes that occur when various alkali metal ions are bound. Structural information is used to assist in the interpretation of the chemical shift changes observed. For d-serine dehydratase, no structural data are available but nevertheless the metal ion arrangement in the PLP binding site can be predicted from 31P NMR data.
AB - The 31P NMR spectroscopy of three pyridoxal 5′-phosphate- dependent enzymes, monomeric d-serine dehydratase, tetrameric dialkylglycine decarboxylase and tetrameric tyrosine phenol-lyase, whose enzymatic activities are dependent on alkali metal ions, was studied. 31P NMR spectra of the latter two enzymes have never been reported, their 3D-structures, however, are available. The cofactor phosphate chemical shift of all three enzymes changes by ∼3 ppm as a function of pH, indicating that the phosphate group changes from being monoanionic at low pH to dianionic at high pH. The 31P NMR signal of the phosphate group of pyridoxal 5′-phosphate provides a measure of the active site changes that occur when various alkali metal ions are bound. Structural information is used to assist in the interpretation of the chemical shift changes observed. For d-serine dehydratase, no structural data are available but nevertheless the metal ion arrangement in the PLP binding site can be predicted from 31P NMR data.
KW - 31P chemical shift
KW - D-serine dehydratase
KW - Dialkylglycine decarboxylase
KW - Monovalent cations
KW - Ppyridoxal 5′-phosphate
KW - Tyrosine phenol-lyase
UR - http://www.scopus.com/inward/record.url?scp=33644543360&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33644543360&partnerID=8YFLogxK
U2 - 10.1016/j.bbapap.2005.10.009
DO - 10.1016/j.bbapap.2005.10.009
M3 - Article
C2 - 16290167
AN - SCOPUS:33644543360
VL - 1764
SP - 230
EP - 238
JO - Biochimica et Biophysica Acta - Proteins and Proteomics
JF - Biochimica et Biophysica Acta - Proteins and Proteomics
SN - 1570-9639
IS - 2
ER -