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Literature summary for 1.5.1.2 extracted from

  • Matsuzawa, T.
    Purification and characterization of pyrroline-5-carboxylate reductase from bovine retina (1982), Biochim. Biophys. Acta, 717, 215-219.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
ATP competitive with respect to NADH, 50% inhibition at 0.1 mM Bos taurus
proline 39% inhibition of the NADH dependent activity and 17% of the NADPH dependent activity at 10 mM Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0071
-
NADPH
-
Bos taurus
0.125
-
1-pyrroline-5-carboxylate
-
Bos taurus
0.2
-
NADH
-
Bos taurus

Metals/Ions

Metals/Ions Comment Organism Structure
KCl 2fold increase at 70 mM Bos taurus
phosphate 10 mM, reaction enhancement Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
retina distribution in bovine cornea and lens Bos taurus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
subcellular distribution Bos taurus
4.167
-
-
Bos taurus

Storage Stability

Storage Stability Organism
-20°C, inactivation in few days, unstable in the absence of NADPH Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-pyrroline-5-carboxylate + NADH + H+
-
Bos taurus L-proline + NAD+
-
r

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 7.5
-
Bos taurus

Cofactor

Cofactor Comment Organism Structure
NADH
-
Bos taurus
NADPH
-
Bos taurus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.1
-
ATP
-
Bos taurus