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Literature summary extracted from

  • Hallen, A.; Jamie, J.; Cooper, A.
    Imine reductases A comparison of glutamate dehydrogenase to ketimine reductases in the brain (2014), Neurochem. Res., 39, 527-541 .
No PubMed abstract available

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.1 DELTA1-piperideine 2-carboxylate + NADPH + H+ Rattus norvegicus
-
 L-pipecolate + NADP+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.1 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.1 native enzyme partially Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.5.1.1 brain
-
 Rattus norvegicus
-
1.5.1.1 kidney
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.1 DELTA1-piperideine 2-carboxylate + NADPH + H+
-
 Rattus norvegicus L-pipecolate + NADP+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.5.1.1 P2C/Pyr2C reductase
-
 Rattus norvegicus
1.5.1.1 P2C/Pyr2C/ketimine reductase
-
 Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.1 NADPH
-
 Rattus norvegicus

General Information

EC Number General Information Comment Organism
1.5.1.1 physiological function the enzymatic reduction of Pyr2C to L-proline together with DAAO may be regarded as a salvage mechanism for converting D-proline, arising from the diet or intestinal bacteria, to L-proline, the more biological useful enantiomer in mammals Rattus norvegicus