Glutamate degradation

Stable Identifier
R-OSA-1119458
Type
Pathway
Species
Oryza sativa
Compartment
Synonyms
GABA shunt, pathway99618, Glutamate degradation III
Locations in the PathwayBrowser
Summation

Glutamate is a major amino donor for the synthesis of amino acids and other nitrogen-containing compounds in plants. Glutamate is converted into ?-Aminobutyric acid (GABA) via glutamate decarboxylase (GAD). Enzymatic activity of GAD may be activated by Ca2+/calmodulin binding at the C-terminus in response to various stresses (Shelp et al., 1999; Bouché and Fromm, 2004). GABA is a non-protein amino acid present in all living things (Bown and Shelp, 1997; Akama et al., 2001). GABA in turn is converted to succinic semialdehyde (SSA) by GABA-transaminase (GABA-T). SSA is catabolized via SSA dehydrogenase (SSADH) to form succinate, which enters the TCA cycle. The route from glutamate to succinate is known as the GABA shunt. Glutamate is known to modulate calcium signaling (Dannison et al., 2000), root system architecture ( Forde & Walch-Liu, 2009), inhibits primary root growth and stimulates the outgrowth of lateral roots near the primary root tip in Arabidopsis (Walch-Liu et al., 2006). This phenomenon is specific to glutamate but other structurally or metabolically related amino acids e.g., Asp, and Gln do not have similar effects (Forde & Walch-Liu, 2009).

Data source: RiceCyc

Literature References
PubMed ID Title Journal Year
12232415 The 58-Kilodalton Calmodulin-Binding Glutamate Decarboxylase Is a Ubiquitous Protein in Petunia Organs and Its Expression Is Developmentally Regulated Plant Physiol. 1994
10517851 Plant succinic semialdehyde dehydrogenase. Cloning, purification, localization in mitochondria, and regulation by adenine nucleotides Plant Physiol. 1999
12740438 Mitochondrial succinic-semialdehyde dehydrogenase of the gamma-aminobutyrate shunt is required to restrict levels of reactive oxygen intermediates in plants Proc. Natl. Acad. Sci. U.S.A. 2003
8626755 Activation of a recombinant petunia glutamate decarboxylase by calcium/calmodulin or by a monoclonal antibody which recognizes the calmodulin binding domain J. Biol. Chem. 1996
23122787 Differential subcellular localization, enzymatic properties and expression patterns of ?-aminobutyric acid transaminases (GABA-Ts) in rice (Oryza sativa) J. Plant Physiol. 2013
26384576 Amino Acid Catabolism in Plants Mol Plant 2015
23421475 Genetic manipulation of the ?-aminobutyric acid (GABA) shunt in rice: overexpression of truncated glutamate decarboxylase (GAD2) and knockdown of ?-aminobutyric acid transaminase (GABA-T) lead to sustained and high levels of GABA accumulation in rice kernels Plant Biotechnol. J. 2013
Metabolism, enzymology and possible roles of 4-aminobutyrate in higher plants Phytochemistry 1990
11779628 Rice (Oryza sativa) contains a novel isoform of glutamate decarboxylase that lacks an authentic calmodulin-binding domain at the C-terminus Biochim. Biophys. Acta 2001
20355097 Purification of calmodulin from rice bran and activation of glutamate decarboxylase by Ca2+/calmodulin J. Sci. Food Agric. 2010
26106401 Closing the loop on the GABA shunt in plants: are GABA metabolism and signaling entwined? Front Plant Sci 2015
24799560 Exogenous ?-aminobutyric acid (GABA) affects pollen tube growth via modulating putative Ca2+-permeable membrane channels and is coupled to negative regulation on glutamate decarboxylase J. Exp. Bot. 2014
28212609 Exogenous glutamate rapidly induces the expression of genes involved in metabolism and defense responses in rice roots BMC Genomics 2017
17578865 Glutamate in plants: metabolism, regulation, and signalling J. Exp. Bot. 2007
11115867 Glutamate-gated calcium fluxes in Arabidopsis Plant Physiol. 2000
15003233 GABA in plants: just a metabolite? Trends Plant Sci. 2004
10529826 Metabolism and functions of gamma-aminobutyric acid Trends Plant Sci. 1999
Participants
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Orthologous Events
Cross References
RiceCyc