Enzymes
UniProtKB help_outline | 6,361 proteins |
Enzyme class help_outline |
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Reaction participants Show >> << Hide
- Name help_outline a 2-oxocarboxylate Identifier CHEBI:35179 Charge -1 Formula C2O3R SMILEShelp_outline [O-]C(=O)C([*])=O 2D coordinates Mol file for the small molecule Search links Involved in 598 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-ornithine Identifier CHEBI:46911 Charge 1 Formula C5H13N2O2 InChIKeyhelp_outline AHLPHDHHMVZTML-BYPYZUCNSA-O SMILEShelp_outline [NH3+]CCC[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 50 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline an L-α-amino acid Identifier CHEBI:59869 Charge 0 Formula C2H4NO2R SMILEShelp_outline [NH3+][C@@H]([*])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 366 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-glutamate 5-semialdehyde Identifier CHEBI:58066 Charge 0 Formula C5H9NO3 InChIKeyhelp_outline KABXUUFDPUOJMW-BYPYZUCNSA-N SMILEShelp_outline [H]C(=O)CC[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 11 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:13877 | RHEA:13878 | RHEA:13879 | RHEA:13880 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Specific form(s) of this reaction
Publications
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An alternative, arginase-independent pathway for arginine metabolism in Kluyveromyces lactis involves guanidinobutyrase as a key enzyme.
Romagnoli G., Verhoeven M.D., Mans R., Fleury Rey Y., Bel-Rhlid R., van den Broek M., Seifar R.M., Ten Pierick A., Thompson M., Muller V., Wahl S.A., Pronk J.T., Daran J.M.
Most available knowledge on fungal arginine metabolism is derived from studies on Saccharomyces cerevisiae, in which arginine catabolism is initiated by releasing urea via the arginase reaction. Orthologues of the S. cerevisiae genes encoding the first three enzymes in the arginase pathway were cl ... >> More
Most available knowledge on fungal arginine metabolism is derived from studies on Saccharomyces cerevisiae, in which arginine catabolism is initiated by releasing urea via the arginase reaction. Orthologues of the S. cerevisiae genes encoding the first three enzymes in the arginase pathway were cloned from Kluyveromyces lactis and shown to functionally complement the corresponding deletion in S. cerevisiae. Surprisingly, deletion of the single K. lactis arginase gene KlCAR1 did not completely abolish growth on arginine as nitrogen source. Growth rate of the deletion mutant strongly increased during serial transfer in shake-flask cultures. A combination of RNAseq-based transcriptome analysis and (13)C-(15)N-based flux analysis was used to elucidate the arginase-independent pathway. Isotopic (13)C(15)N-enrichment in γ-aminobutyrate revealed succinate as the entry point in the TCA cycle of the alternative pathway. Transcript analysis combined with enzyme activity measurements indicated increased expression in the Klcar1Δ mutant of a guanidinobutyrase (EC.3.5.3.7), a key enzyme in a new pathway for arginine degradation. Expression of the K. lactis KLLA0F27995g (renamed KlGBU1) encoding guanidinobutyrase enabled S. cerevisiae to use guanidinobutyrate as sole nitrogen source and its deletion in K. lactis almost completely abolish growth on this nitrogen source. Phylogenetic analysis suggests that this enzyme activity is widespread in fungi. << Less
Mol. Microbiol. 93:369-389(2014) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Isolation of the ornithine-delta-aminotransferase cDNA and effect of salt stress on its expression in Arabidopsis thaliana.
Roosens N.H., Thu T.T., Iskandar H.M., Jacobs M.
To evaluate the relative importance of ornithine (Orn) as a precursor in proline (Pro) synthesis, we isolated and sequenced a cDNA encoding the Orn-delta-aminotransferase (delta-OAT) from Arabidopsis thaliana. The deduced amino acid sequence showed high homology with bacterial, yeast, mammalian, a ... >> More
To evaluate the relative importance of ornithine (Orn) as a precursor in proline (Pro) synthesis, we isolated and sequenced a cDNA encoding the Orn-delta-aminotransferase (delta-OAT) from Arabidopsis thaliana. The deduced amino acid sequence showed high homology with bacterial, yeast, mammalian, and plant sequences, and the N-terminal residues exhibited several common features with a mitochondrial transit peptide. Our results show that under both salt stress and normal conditions, delta-OAT activity and mRNA in young plantlets are slightly higher than in older plants. This appears to be related to the necessity to dispose of an easy recycling product, glutamate. Analysis of the expression of the gene revealed a close association with salt stress and Pro production. In young plantlets, free Pro content, Delta1-pyrroline-5-carboxylate synthase mRNA, delta-OAT activity, and delta-OAT mRNA were all increased by salt-stress treatment. These results suggest that for A. thaliana, the Orn pathway, together with the glutamate pathway, plays an important role in Pro accumulation during osmotic stress. Conversely, in 4-week-old A. thaliana plants, although free Pro level also increased under salt-stress conditions, the delta-OAT activity appeared to be unchanged and delta-OAT mRNA was not detectable. Delta1-pyrroline-5-carboxylate synthase mRNA was still induced at a similar level. Therefore, for the adult plants the free Pro increase seemed to be due to the activity of the enzymes of the glutamate pathway. << Less