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Chemical Compound Review:

CHEMBL18591 4,5-dihydro-3H-pyrrole-2- carboxylic acid

Synonyms: SureCN142379, AG-E-56684, SureCN4314360, SureCN9835844, CHEBI:36761, ...

Garweg, G. et al., Fisher, H.F. et al., Pirrung, M.C. et al., Satomura, T. et al.

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High impact information on delta1-Pyrroline 2-carboxylate

We report here the glutamate dehydrogenase catalyzed reduction of delta 1-pyrroline-2-carboxylic acid (a cyclic-alpha-imino acid) to proline (an alpha-amino acid) [1].
RESULTS: ACBC was converted to dehydroproline (delta 1-pyrroline-2-carboxylic acid) by the EFE via a ring expansion process [2].
L-Pipecolate formation exhibits considerable regional differences in the central nervous system of the mouse, dog, and monkey, as reflected in measurements of the activity of delta1-pyrroline-2-carboxylate reductase (D.C. 1.5.1.1) [3].
In addition to delta1-piperidine-2-carboxylate, delta1-pyrroline-2-carboxylate was also found to be a substrate for the same enzyme in homogenates of mouse forebrain [3].

Associations of delta1-Pyrroline 2-carboxylate with other chemical compounds

Glutamate dehydrogenase catalyzes the reduction of a Schiff base (delta 1-pyrroline-2-carboxylic acid) by NADPH [1].

Analytical, diagnostic and therapeutic context of delta1-Pyrroline 2-carboxylate

Delta(1)-Pyrroline-2-carboxylate was identified as the reaction product from d-proline by thin layer chromatography [4].

References

Glutamate dehydrogenase catalyzes the reduction of a Schiff base (delta 1-pyrroline-2-carboxylic acid) by NADPH. Fisher, H.F., Srinivasan, R., Rougvie, A.E. J. Biol. Chem. (1982) [Pubmed]
Ethylene biosynthesis: processing of a substrate analog supports a radical mechanism for the ethylene-forming enzyme. Pirrung, M.C., Cao, J., Chen, J. Chem. Biol. (1998) [Pubmed]
L-Pipecolate formation in the mammalian brain. Regional distribution of delta1-pyrroline-2-carboxylate reductase activity. Garweg, G., von Rehren, D., Hintze, U. J. Neurochem. (1980) [Pubmed]
Dye-linked D-proline dehydrogenase from hyperthermophilic archaeon Pyrobaculum islandicum is a novel FAD-dependent amino acid dehydrogenase. Satomura, T., Kawakami, R., Sakuraba, H., Ohshima, T. J. Biol. Chem. (2002) [Pubmed]

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