Reaction participants Show >> << Hide
- Name help_outline 2-oxobutanoate Identifier CHEBI:16763 (Beilstein: 3601760) help_outline Charge -1 Formula C4H5O3 InChIKeyhelp_outline TYEYBOSBBBHJIV-UHFFFAOYSA-M SMILEShelp_outline CCC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 33 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-alanine Identifier CHEBI:57972 Charge 0 Formula C3H7NO2 InChIKeyhelp_outline QNAYBMKLOCPYGJ-REOHCLBHSA-N SMILEShelp_outline C[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 107 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (2S)-2-aminobutanoate Identifier CHEBI:74359 Charge 0 Formula C4H9NO2 InChIKeyhelp_outline QWCKQJZIFLGMSD-VKHMYHEASA-N SMILEShelp_outline CC[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 15 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline pyruvate Identifier CHEBI:15361 (Beilstein: 3587721; CAS: 57-60-3) help_outline Charge -1 Formula C3H3O3 InChIKeyhelp_outline LCTONWCANYUPML-UHFFFAOYSA-M SMILEShelp_outline CC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 213 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:77355 | RHEA:77356 | RHEA:77357 | RHEA:77358 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Dimethylarginine:pyruvate aminotransferase in rats. Purification, properties, and identity with alanine:glyoxylate aminotransferase 2.
Ogawa T., Kimoto M., Sasaoka K.
Dimethylarginine:pyruvate aminotransferase, which plays a role in the metabolism of dimethylarginines, has been purified to homogeneity from rat kidney. The enzyme has a molecular weight of approximately 200,000 and an isoelectric point at about pH 6.3. The enzyme consists of four similar subunits ... >> More
Dimethylarginine:pyruvate aminotransferase, which plays a role in the metabolism of dimethylarginines, has been purified to homogeneity from rat kidney. The enzyme has a molecular weight of approximately 200,000 and an isoelectric point at about pH 6.3. The enzyme consists of four similar subunits having a molecular weight of about 50,000. The enzyme catalyzes the effective transaminations of guanidino-N methylated L-arginines (e.g. NG,NG-dimethyl-L-arginine, NG,N'G-dimethyl-L-arginine and NG-monomethyl-L-arginine) and the alpha-amino group of L-ornithine to pyruvate or glyoxylate. The enzyme was always accompanied by the known alanine:glyoxylate amino-transferase activity with the ratios of their specific activities remaining constant during the purification steps. The physicochemical and immunological properties of the purified enzyme were shown to be identical with those of the isozyme of alanine:glyoxylate aminotransferase (EC 2.6.1.44), designated as alanine:glyoxylate aminotransferase 2 (Noguchi, T. (1987) in Peroxisomes in Biology and Medicine (Fahimi, H. D., and Sies, H., eds) pp. 234-243, Springer-Verlag, Heidelberg). The distribution profiles in tissues and the negative response to glucagon treatment further supported the identity of the two enzymes. The present data show that alanine:glyoxilate aminotransferase 2 functions in dimethylarginine metabolism in vivo in rats. << Less
J. Biol. Chem. 265:20938-20945(1990) [PubMed] [EuropePMC]
This publication is cited by 15 other entries.