Structural highlights
Function
GLYR1_ARATH Catalyzes the NADPH-dependent reduction of glyoxylate to glycolate as well as succinic semialdehyde (SSA) to gamma-hydroxybutyrate in vitro. May function in redox homeostasis and play a role in oxidative stress tolerance by detoxifying glyoxylate and SSA generated in glycolate metabolism and GABA metabolism, respectively.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Breitkreuz KE, Allan WL, Van Cauwenberghe OR, Jakobs C, Talibi D, Andre B, Shelp BJ. A novel gamma-hydroxybutyrate dehydrogenase: identification and expression of an Arabidopsis cDNA and potential role under oxygen deficiency. J Biol Chem. 2003 Oct 17;278(42):41552-6. Epub 2003 Jul 25. PMID:12882961 doi:http://dx.doi.org/10.1074/jbc.M305717200
- ↑ Bienvenut WV, Sumpton D, Martinez A, Lilla S, Espagne C, Meinnel T, Giglione C. Comparative large scale characterization of plant versus mammal proteins reveals similar and idiosyncratic N-alpha-acetylation features. Mol Cell Proteomics. 2012 Jun;11(6):M111.015131. doi: 10.1074/mcp.M111.015131., Epub 2012 Jan 5. PMID:22223895 doi:http://dx.doi.org/10.1074/mcp.M111.015131
- ↑ Ching SL, Gidda SK, Rochon A, van Cauwenberghe OR, Shelp BJ, Mullen RT. Glyoxylate reductase isoform 1 is localized in the cytosol and not peroxisomes in plant cells. J Integr Plant Biol. 2012 Mar;54(3):152-68. doi:, 10.1111/j.1744-7909.2012.01103.x. PMID:22309191 doi:http://dx.doi.org/10.1111/j.1744-7909.2012.01103.x
