Enzymes
| UniProtKB help_outline | 250 proteins |
| Enzyme class help_outline |
|
Reaction participants Show >> << Hide
- Name help_outline 4-aminobutanoate Identifier CHEBI:59888 Charge 0 Formula C4H9NO2 InChIKeyhelp_outline BTCSSZJGUNDROE-UHFFFAOYSA-N SMILEShelp_outline [NH3+]CCCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 23 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline glyoxylate Identifier CHEBI:36655 (Beilstein: 3903641) help_outline Charge -1 Formula C2HO3 InChIKeyhelp_outline HHLFWLYXYJOTON-UHFFFAOYSA-M SMILEShelp_outline [H]C(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 88 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline succinate semialdehyde Identifier CHEBI:57706 Charge -1 Formula C4H5O3 InChIKeyhelp_outline UIUJIQZEACWQSV-UHFFFAOYSA-M SMILEShelp_outline [O-]C(=O)CCC=O 2D coordinates Mol file for the small molecule Search links Involved in 17 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline glycine Identifier CHEBI:57305 Charge 0 Formula C2H5NO2 InChIKeyhelp_outline DHMQDGOQFOQNFH-UHFFFAOYSA-N SMILEShelp_outline [NH3+]CC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 152 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:32267 | RHEA:32268 | RHEA:32269 | RHEA:32270 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
|||
| EC numbers help_outline | ||||
| KEGG help_outline | ||||
| MetaCyc help_outline |
Publications
-
Subcellular localization and expression of multiple tomato gamma-aminobutyrate transaminases that utilize both pyruvate and glyoxylate.
Clark S.M., Di Leo R., Van Cauwenberghe O.R., Mullen R.T., Shelp B.J.
Gamma-aminobutyric acid transaminase (GABA-T) catalyses the breakdown of GABA to succinic semialdehyde. In this report, three GABA-T isoforms were identified in the tomato (Solanum lycopersicum L.) plant. The deduced amino acid sequences of the three isoforms are highly similar over most of their ... >> More
Gamma-aminobutyric acid transaminase (GABA-T) catalyses the breakdown of GABA to succinic semialdehyde. In this report, three GABA-T isoforms were identified in the tomato (Solanum lycopersicum L.) plant. The deduced amino acid sequences of the three isoforms are highly similar over most of their coding regions with the exception of their N-terminal regions. Transient expression of the individual full-length GABA-T isoforms fused to the green fluorescent protein in tobacco suspension-cultured cells revealed their distinct subcellular localizations to the mitochondrion, plastid or cytosol, and that the specific targeting of the mitochondrion- and plastid-localized isoforms is mediated by their predicted N-terminal presequences. Removal of the N-terminal targeting presequences from the mitochondrion and plastid GABA-T isoforms yielded good recovery of the soluble recombinant proteins in Escherichia coli when they were co-expressed with the GroES/EL molecular chaperone complex. Activity assays indicated that all three recombinant isoforms possess both pyruvate- and glyoxylate-dependent GABA-T activities, although the mitochondrial enzyme has a specific activity that is significantly higher than that of its plastid and cytosolic counterparts. Finally, differential expression patterns of the three GABA-T isoforms in reproductive tissues, but not vegetative tissues, suggest unique roles for each enzyme in developmental processes. Overall, these findings, together with recent information about rice and pepper GABA-Ts, indicate that the subcellular distribution of GABA-T in the plant kingdom is highly variable. << Less
J. Exp. Bot. 60:3255-3267(2009) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
-
Biochemical characterization, mitochondrial localization, expression, and potential functions for an Arabidopsis gamma-aminobutyrate transaminase that utilizes both pyruvate and glyoxylate.
Clark S.M., Di Leo R., Dhanoa P.K., Van Cauwenberghe O.R., Mullen R.T., Shelp B.J.
Gamma-aminobutyrate transaminase (GABA-T) catalyses the breakdown of GABA to succinic semialdehyde. In this report, the previously identified Arabidopsis thaliana (L.) Heyhn GABA-T (AtGABA-T) was characterized in more detail. Full-length AtGABA-T contains an N-terminal 36 amino acid long targeting ... >> More
Gamma-aminobutyrate transaminase (GABA-T) catalyses the breakdown of GABA to succinic semialdehyde. In this report, the previously identified Arabidopsis thaliana (L.) Heyhn GABA-T (AtGABA-T) was characterized in more detail. Full-length AtGABA-T contains an N-terminal 36 amino acid long targeting pre-sequence (36 amino acids) that is both sufficient and necessary for targeting the enzyme to mitochondria. Removal of the pre-sequence encoding this N-terminal targeting domain and co-expression of the resulting truncated AtGABA-T cDNA with the GroES/EL molecular chaperone complex in Escherichia coli yielded good recovery of the soluble recombinant proteins. Activity assays indicated that purified recombinant GABA-T has both pyruvate- and glyoxylate-dependent activities, but cannot utilize 2-oxoglutarate as amino acceptor. Kinetic parameters for glyoxylate- and pyruvate-dependent GABA-T activities were similar, with physiologically relevant affinities. Assays of GABA-T activity in cell-free leaf extracts from wild-type Arabidopsis and two knockout mutants in different genetic backgrounds confirmed that the native enzyme possesses both pyruvate- and glyoxylate-dependent activities. The GABA-T transcript was present throughout the plant, but its expression was highest in roots and increased as a function of leaf development. A GABA-T with dual functions suggests the potential for interaction between GABA metabolism and photorespiratory glyoxylate production. << Less
J. Exp. Bot. 60:1743-1757(2009) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.