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Literature summary for 1.5.1.2 extracted from

  • Costilow, R.N.; Cooper, D.
    Identity of proline dehydrogenase and delta1-pyrroline-5-carboxylic acid reductase in Clostridium sporogenes (1978), J. Bacteriol., 134, 139-146.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.33
-
L-pyrroline-5-carboxylate pH 8.0 Clostridium sporogenes
0.33
-
L-pyrroline-5-carboxylate pH 6.5 Clostridium sporogenes
1 1.2 NAD+
-
Clostridium sporogenes
1.25
-
L-proline pH 10.2 Clostridium sporogenes
31
-
L-proline pH 8.0 Clostridium sporogenes

Organism

Organism UniProt Comment Textmining
Clostridium sporogenes
-
-
-

Purification (Commentary)

Purification (Comment) Organism
copurification with proline oxidase, both activities located on the same protein Clostridium sporogenes

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
70.1
-
-
Clostridium sporogenes

Storage Stability

Storage Stability Organism
-18°C, 0.15-0.2 M potassium phosphate buffer pH 7.4, 2 months Clostridium sporogenes

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-pyrroline-5-carboxylate + NAD(P)H + H+ specific for L-isomer Clostridium sporogenes L-proline + NAD(P)+
-
?
1-pyrroline-5-carboxylate + NADH + H+
-
Clostridium sporogenes L-proline + NAD+
-
r
L-proline + NAD+
-
Clostridium sporogenes 1-pyrroline-5-carboxylate + NADH + H+
-
r

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
10 min, complete inactivation Clostridium sporogenes

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5 7.5
-
Clostridium sporogenes
10.2
-
proline dehydrogenase activity Clostridium sporogenes

Cofactor

Cofactor Comment Organism Structure
NADH
-
Clostridium sporogenes
NADPH no reaction Clostridium sporogenes