ArticleThe Journal of biological chemistry2013
Structure of the homodimeric glycine decarboxylase P-protein from Synechocystis sp. PCC 6803 suggests a mechanism for redox regulation.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 41 citations in OpenAlex.
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- Pathogenic variants in GCSH encoding the moonlighting H-protein cause combined nonketotic hyperglycinemia and lipoate deficiency.Human molecular genetics · 2023Article
- Understanding and Engineering Glycine Cleavage System and Related Metabolic Pathways for C1-Based Biosynthesis.Advances in biochemical engineering/biotechnology · 2022Review
- Improvement of glycine biosynthesis from one-carbon compounds and ammonia catalyzed by the glycine cleavage system in vitro.Engineering in life sciences · 2022Article
- mTORC1 activity regulates post-translational modifications of glycine decarboxylase to modulate glycine metabolism and tumorigenesis.Nature communications · 2021Article
- Genomic analyses of glycine decarboxylase neurogenic mutations yield a large-scale prediction model for prenatal disease.PLoS genetics · 2021Article
- Large scale analyses of genotype-phenotype relationships of glycine decarboxylase mutations and neurological disease severity.PLoS computational biology · 2020Article
- Redox-Regulation of Photorespiration through Mitochondrial Thioredoxin o1.Plant physiology · 2019Article
- Article
- The genetic basis of classic nonketotic hyperglycinemia due to mutations in GLDC and AMT.Genetics in medicine : official journal of the American College of Medical Genetics · 2017Article
- Identification of a RAI1-associated disease network through integration of exome sequencing, transcriptomics, and 3D genomics.Genome medicine · 2016Article
- Discovery of a sesamin-metabolizing microorganism and a new enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Structure of the PLP-Form of the Human Kynurenine Aminotransferase II in a Novel Spacegroup at 1.83 Å Resolution.International journal of molecular sciences · 2016Article
- A Shortest-Path-Based Method for the Analysis and Prediction of Fruit-Related Genes in Arabidopsis thaliana.PloS one · 2016Article
- Biochemical and molecular predictors for prognosis in nonketotic hyperglycinemia.Annals of neurology · 2015Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycine decarboxylase, or P-protein, is a pyridoxal 5'-phosphate (PLP)-dependent enzyme in one-carbon metabolism of all organisms, in the glycine and serine catabolism of vertebrates, and in the photorespiratory pathway of oxygenic phototrophs. P-protein from the cyanobacterium Synechocystis sp. PCC 6803 is an α2 homodimer with high homology to eukaryotic P-proteins. The crystal structure of the apoenzyme shows the C terminus locked in a closed conformation by a disulfide bond between Cys(972) in the C terminus and Cys(353) located in the active site. The presence of the disulfide bridge isolates the active site from solvent and hinders the binding of PLP and glycine in the active site. Variants produced by substitution of Cys(972) and Cys(353) by Ser using site-directed mutagenesis have distinctly lower specific activities, supporting the crucial role of these highly conserved redox-sensitive amino acid residues for P-protein activity. Reduction of the 353-972 disulfide releases the C terminus and allows access to the active site. PLP and the substrate glycine bind in the active site of this reduced enzyme and appear to cause further conformational changes involving a flexible surface loop. The observation of the disulfide bond that acts to stabilize the closed form suggests a molecular mechanism for the redox-dependent activation of glycine decarboxylase observed earlier.
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