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Literature summary for 1.5.1.2 extracted from

  • Forlani, G.; Nocek, B.; Ruszkowski, M.
    Peculiar substrate specificity of delta1-pyrroline-5-carboxylate reductase in the obligately fermentative bacterium Zymomonas mobilis (2021), Mol. Biol. Rep., 48, 6205-6211 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Zymomonas mobilis subsp. mobilis

Inhibitors

Inhibitors Comment Organism Structure
L-proline
-
Zymomonas mobilis subsp. mobilis
NaCl
-
Zymomonas mobilis subsp. mobilis
NAD+
-
Zymomonas mobilis subsp. mobilis
NADP+
-
Zymomonas mobilis subsp. mobilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.135
-
NADH pH 7.5, 30°C Zymomonas mobilis subsp. mobilis
0.273
-
1-pyrroline-5-carboxylate cosubstrate NADH, pH 7.5, 30°C Zymomonas mobilis subsp. mobilis
0.719
-
NADPH pH 7.5, 30°C Zymomonas mobilis subsp. mobilis
1.053
-
1-pyrroline-5-carboxylate cosubstrate NADPH, pH 7.5, 30°C Zymomonas mobilis subsp. mobilis

Organism

Organism UniProt Comment Textmining
Zymomonas mobilis subsp. mobilis Q5NQR9
-
-
Zymomonas mobilis subsp. mobilis ATCC 31821 Q5NQR9
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
9.3
-
substrate NADPH, pH 7.5, 30°C Zymomonas mobilis subsp. mobilis
36.53
-
substrate NADH, pH 7.5, 30°C Zymomonas mobilis subsp. mobilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-pyrroline-5-carboxylate + NADH + H+
-
Zymomonas mobilis subsp. mobilis L-proline + NAD+
-
?
1-pyrroline-5-carboxylate + NADH + H+
-
Zymomonas mobilis subsp. mobilis ATCC 31821 L-proline + NAD+
-
?
1-pyrroline-5-carboxylate + NADPH + H+
-
Zymomonas mobilis subsp. mobilis L-proline + NADP+
-
?
1-pyrroline-5-carboxylate + NADPH + H+
-
Zymomonas mobilis subsp. mobilis ATCC 31821 L-proline + NADP+
-
?

Synonyms

Synonyms Comment Organism
PROC
-
Zymomonas mobilis subsp. mobilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6
-
NADPH pH 7.5, 30°C Zymomonas mobilis subsp. mobilis
27
-
NADH pH 7.5, 30°C Zymomonas mobilis subsp. mobilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
and 7.7 Zymomonas mobilis subsp. mobilis
7.6
-
and 6.5 Zymomonas mobilis subsp. mobilis

Cofactor

Cofactor Comment Organism Structure
NADH maximal activity is evident with cofactor NADH Zymomonas mobilis subsp. mobilis
NADPH higher affinity for NADPH than NADH Zymomonas mobilis subsp. mobilis

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.4
-
substrate NADPH, pH 7.5, 30°C Zymomonas mobilis subsp. mobilis NAD+
7.4
-
substrate NADH, pH 7.5, 30°C Zymomonas mobilis subsp. mobilis NAD+
22.6
-
substrate NADH, pH 7.5, 30°C Zymomonas mobilis subsp. mobilis NADP+
96
-
substrate NADH, pH 7.5, 30°C Zymomonas mobilis subsp. mobilis L-proline
107
-
substrate NADPH, pH 7.5, 30°C Zymomonas mobilis subsp. mobilis L-proline
130
-
substrate NADPH, pH 7.5, 30°C Zymomonas mobilis subsp. mobilis NaCl
1144
-
substrate NADH, pH 7.5, 30°C Zymomonas mobilis subsp. mobilis NaCl

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
8.4
-
NADPH pH 7.5, 30°C Zymomonas mobilis subsp. mobilis
196
-
NADH pH 7.5, 30°C Zymomonas mobilis subsp. mobilis