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.

Reaction

Synonyms

1-pyrroline-5-carboxylate reductase, aldimine reductase, DELTA1-pyrroline-5-carboxylate reductase, DELTA1-pyrroline-5-carboxylate reductase 2, 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, PROC, proline oxidase, Pycr1, PYCR2, Pyr5C reductase, pyrroline-5-carboxylate dehydrogenase, pyrroline-5-carboxylate reductase, reductase, pyrroline-5-carboxylate, TcCLB.509207.90

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

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Results	in table
8	Activating Compound
45977	AA Sequence
9	Application
1	CAS Registry Number
23	Cloned(Commentary)
92	Cofactor
8	Crystallization (Commentary)
535	Disease/ Diagnostics
4	Expression
12	General Information
6	General Stability
67	IC50 Value
175	Inhibitors
33	kcat/KM [mM/s]
11	Ki Value [mM]
127	KM Value [mM]
25	Localization
14	Metals/Ions
27	Molecular Weight [Da]
41	Natural Substrates/ Products (Substrates)
116	Organism
9	Pathway
128	PDB ID
41	pH Optimum
7	pH Range
3	pH Stability
1	pI Value
9	Protein Variants
32	Purification (Commentary)
2	Reaction
27	Reaction Type
100	Reference
1	Renatured (Commentary)
82	Source Tissue
42	Specific Activity [micromol/min/mg]
12	Storage Stability
140	Substrates and Products (Substrate)
18	Subunits
70	Synonyms
1	Systematic Name
9	Temperature Optimum [°C]
1	Temperature Range [°C]
17	Temperature Stability [°C]
52	Turnover Number [1/s]

Crystallization

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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

Homo sapiens

-

675382

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

Homo sapiens

P32322

740763

PYCR1 complexed with N-formyl-L-proline, inhibitor binding is accompanied by conformational changes in the active site, including the translation of an alpha-helix by 1 A

Homo sapiens

P32322

763270

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

Homo sapiens

P32322

676969

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

Medicago truncatula

G7KRM5

740491

crystal structure is determined at 2.0 A resolution, in complex with NADP+ at 2.1 A resolution

Neisseria meningitidis

-

675361

diffraction to 3.5 A resolution

Saccharolobus solfataricus

Q97ZT3

701063

crystal structure is determined at 2.15 A resolution in complex with NADP+, and at 2.20 A in complex with L-proline

Streptococcus pyogenes

-

675361