1.5.1.2: pyrroline-5-carboxylate reductase

This is an abbreviated version!
For detailed information about pyrroline-5-carboxylate reductase, go to the full flat file.

Word Map on EC 1.5.1.2

Reaction

L-proline
+
NAD(P)+
=
1-pyrroline-5-carboxylate
+
NAD(P)H
+
H+

Synonyms

1-pyrroline-5-carboxylate reductase, DELTA1-pyrroline-5-carboxylate reductase, L-proline oxidase, L-proline-NAD(P)+ 5-oxidoreductase, L-proline:NAD(P)+ 5-oxidoreductase, MTR_7g090160, NADPH-L-DELTA'-pyrroline carboxylic acid reductase, P5C reductase, P5CDH, P5CR, PO, POX, proline oxidase, Pycr1, pyrroline-5-carboxylate dehydrogenase, pyrroline-5-carboxylate reductase, reductase, pyrroline-5-carboxylate

ECTree

     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.1 With NAD+ or NADP+ as acceptor
                1.5.1.2 pyrroline-5-carboxylate reductase

Crystallization

Crystallization on EC 1.5.1.2 - pyrroline-5-carboxylate reductase

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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
2.8 A resolution structure of the pyrroline-5-carboxylate reductase apo enzyme, and its ternary complex with NADPH and substrate analog at 3.1 A
-
binary complexes of PYCR1 with NADPH or proline, at 1.9 A resolution, and a ternary complex containing NADPH and a P5C/proline analog, to 1.85 A resolution. NADPH is bound to the Rossmann fold. Structures provide a model of the Michaelis complex formed during hydride transfer
-
the protein is crystallized by the hanging-drop vapor-diffusion method at 37°C and diffraction data are obtained to a resolution of 2.8 A
-
crystal structures of unliganded P5CR decamer, and its complexes with the products NAD+, NADP+, and L-proline, to 1.7, 1.85, 1.95, and 2.1 A resolution, respectively
crystal structure is determined at 2.0 A resolution, in complex with NADP+ at 2.1 A resolution
-
diffraction to 3.5 A resolution
crystal structure is determined at 2.15 A resolution in complex with NADP+, and at 2.20 A in complex with L-proline
-