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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
Published on: May 3, 2018
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Human serine racemase is nitrosylated at multiple sites
Francesco Marchesani1, Stefano Bruno1, Gianluca Paredi1
1Dipartimento di Scienze degli Alimenti e del Farmaco, Università di Parma, Parma, Italy.
Biochimica Et Biophysica Acta. Proteins and Proteomics
|February 8, 2018
Summary
Human serine racemase inhibition by S-nitrosylation is biphasic, involving Cys113, Cys128, and unique Cys269. This conformational change, not ATP displacement, modulates enzyme activity.
Area of Science:
- Biochemistry
- Enzymology
- Neuroscience
Background:
- Serine racemase synthesizes d-serine, a key NMDA receptor neuromodulator.
- Enzyme activity is regulated by ligands like ATP and cations.
- Murine serine racemase is inhibited by S-nitrosylation at Cys113.
Purpose of the Study:
- Investigate the mechanism of human serine racemase inhibition by S-nitrosylation.
- Identify specific S-nitrosylation sites and their functional consequences.
- Elucidate the structural basis of enzyme regulation.
Main Methods:
- Mass spectrometry to identify S-nitrosylation sites.
- Site-directed mutagenesis to confirm cysteine residue involvement.
- Fluorescence spectroscopy to monitor conformational changes.
Main Results:
- Human serine racemase exhibits biphasic S-nitrosylation inhibition kinetics.
- Cys113, Cys128, and unique human Cys269 are identified as S-nitrosylation sites.
- S-nitrosylation causes partial disruption of ATP-active site communication.
Conclusions:
- Human serine racemase inhibition involves multiple cysteine residues.
- S-nitrosylation induces conformational changes affecting enzyme activity.
- Regulation differs between human and murine serine racemase orthologues.
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