Enzymes
UniProtKB help_outline | 977 proteins |
Reaction participants Show >> << Hide
- Name help_outline L-threonyl-L-threonine Identifier CHEBI:169953 Charge 0 Formula C8H16N2O5 InChIKeyhelp_outline DSGIVWSDDRDJIO-ZXXMMSQZSA-N SMILEShelp_outline C[C@@H](O)[C@H]([NH3+])C(=O)N[C@@H]([C@@H](C)O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,264 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-threonine Identifier CHEBI:57926 Charge 0 Formula C4H9NO3 InChIKeyhelp_outline AYFVYJQAPQTCCC-GBXIJSLDSA-N SMILEShelp_outline C[C@@H](O)[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 32 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:67360 | RHEA:67361 | RHEA:67362 | RHEA:67363 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
UniProtKB help_outline |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Family-wide Annotation of Enzymatic Pathways by Parallel In Vivo Metabolomics.
Kim J.T., Li V.L., Terrell S.M., Fischer C.R., Long J.Z.
Enzymes catalyze fundamental biochemical reactions that control cellular and organismal homeostasis. Here we present an approach for de novo biochemical pathway discovery across entire mammalian enzyme families using parallel viral transduction in mice and untargeted liquid chromatography-mass spe ... >> More
Enzymes catalyze fundamental biochemical reactions that control cellular and organismal homeostasis. Here we present an approach for de novo biochemical pathway discovery across entire mammalian enzyme families using parallel viral transduction in mice and untargeted liquid chromatography-mass spectrometry. Applying this method to the M20 peptidases uncovers both known pathways of amino acid metabolism as well as a previously unknown CNDP2-regulated pathway for threonyl dipeptide catabolism. Ablation of CNDP2 in mice elevates threonyl dipeptides across multiple tissues, establishing the physiologic relevance of our biochemical assignments. Taken together, these data underscore the utility of parallel in vivo metabolomics for the family-wide discovery of enzymatic pathways. << Less
Cell Chem. Biol. 26:1623-1629(2019) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.