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Literature summary extracted from

  • Meng, Z.; Lou, Z.; Liu, Z.; Li, M.; Zhao, X.; Bartlam, M.; Rao, Z.
    Crystal structure of human pyrroline-5-carboxylate reductase (2006), J. Mol. Biol., 359, 1364-1377.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.1.2 cloned into the pET28a+ vector with a His6 tag at the N-terminus for expression in the Escherichia coli strain B834DE3 Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.5.1.2 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

Protein Variants

EC Number Protein Variants Comment Organism
1.5.1.2 E221A affinity for substrates is increased Homo sapiens
1.5.1.2 E221G insoluble protein Homo sapiens
1.5.1.2 additional information N-truncation results in an insoluble protein, C-truncation does not alter the activity Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.1.2 proline competitive inhibitor of P5CR NAD(P)H-dependent thioproline dehydrogenase activity Homo sapiens
1.5.1.2 stearoyl-CoA competitive inhibitor of P5CR NAD(P)H-dependent thioproline dehydrogenase activity Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.2 0.151
-
 NAD+ wild type enzyme, 1 mM fixed thioproline, thioproline dehydrogenase activity assay Homo sapiens
1.5.1.2 0.235
-
 NAD+ E221A mutant, 1 mM fixed thioproline, thioproline dehydrogenase activity assay Homo sapiens
1.5.1.2 0.48
-
 NADP+ E221A mutant, 1 mM fixed thioproline, thioproline dehydrogenase activity assay Homo sapiens
1.5.1.2 0.73
-
 NADP+ E221A mutant, fixed 1 mM NADP+ Homo sapiens
1.5.1.2 1.26
-
 NADP+ wild type enzyme, fixed 1 mM NADP+ Homo sapiens
1.5.1.2 3.06
-
 NADP+ wild type enzyme, 1 mM fixed thioproline, thioproline dehydrogenase activity assay Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.2 L-proline + NAD(P)+ Homo sapiens
-
 1-pyrroline-5-carboxylate + NAD(P)H + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.2 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.2 using a Ni-NTA agarose, a Superdex200 and a Resource Q column Homo sapiens

Renatured (Commentary)

EC Number Renatured (Comment) Organism
1.5.1.2 refolding after treatment with urea Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.2 L-proline + NAD(P)+
-
 Homo sapiens 1-pyrroline-5-carboxylate + NAD(P)H + H+
-
 r

Subunits

EC Number Subunits Comment Organism
1.5.1.2 decamer five homodimer subunits Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.5.1.2 P5CR
-
 Homo sapiens
1.5.1.2 pyrroline-5-carboxylate reductase
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.1.2 25
-
 activity assay Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.5.1.2 13
-
 NADP+ E221A mutant, fixed 1 mM NADP+ Homo sapiens
1.5.1.2 55
-
 NADP+ wild type enzyme, fixed 1 mM NADP+ Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.1.2 9
-
 activity assay Homo sapiens
1.5.1.2 10
-
 L-proline dehydrogenase activity assay Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.2 NAD+
-
 Homo sapiens
1.5.1.2 NADH
-
 Homo sapiens
1.5.1.2 NADP+
-
 Homo sapiens
1.5.1.2 NADPH
-
 Homo sapiens