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1-pyrroline-5-carboxylate + NAD(P)+ + H2O
L-glutamate + NAD(P)H
-
-
-
-
?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH + H+
1-pyrroline-5-carboxylate + NADH + H+
L-proline + NAD+
-
-
-
?
1-pyrroline-5-carboxylate + NADP+ + H2O
L-glutamate + NADPH
-
-
-
-
?
1-pyrroline-5-carboxylate + NADP+ + H2O
L-glutamate + NADPH + H+
2-aminoadipic semialdehyde + NAD+ + H2O
2-aminoadipate + NADH + H+
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + H+
3-methoxybenzaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH
-
as active as 1-pyrroline-5-carboxylate with isoform A, no activity with isoform B
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
4-methoxybenzaldehyde + NAD+ + H2O
4-methoxybenzoate + NADH + H+
-
as active as 1-pyrroline-5-carboxylate with isoform A, no activity with isoform B
-
-
?
4-nitrobenzaldehyde + NAD+ + H2O
4-nitrobenzoate + NADH + H+
-
as active as 1-pyrroline-5-carboxylate with isoform A, only slight activity with isoform B
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
41% activity compared to 1-pyrroline-5-carboxylate with isoform A, only slight activity with isoform B
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
2fold higher activity than with 1-pyrroline-5-carboxylate, isoform A, only slight activity with isoform B
-
-
?
D-glucose + NAD+ + H2O
D-gluconate + NADH
-
80% of the activity with 1-pyrroline-5-carboxylate with isoform A, no activity with isoform B
-
-
?
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + H+
DELTA1-pyrroline-3-hydroxy-5-carboxylate + NAD+ + H2O
4-hydroxyglutamate + NADH
formaldehyde + NAD+ + H2O
formate + NADH
-
50% of activity with 1-pyrroline-5-carboxylate, isoform A, only slight activity with isoform B
-
-
?
glutaric semialdehyde + NAD+ + H2O
glutarate + NADH + H+
glyceralaldehyde-3-phosphate + NAD+ + H2O
glycerate-3-phosphate + NADH
-
slight activity with isoforms A and B
-
-
?
glyoxylic acid + NAD+ + H2O
oxalic acid + NADH
-
41% activity of that with 1-pyrroline-5-carboxylate with isoform A, no activity with isoform B
-
-
?
indole-3-acetaldehyde + NAD+ + H2O
indole-3-acetate + NADH + H+
-
66% activity of that with 1-pyrroline-5-carboxylate with isoform A, only slight activity with isoform B
-
-
?
indole-3-phosphate + NAD+ + H2O
?
-
slight activity with isoforms A and B
-
-
?
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
L-glutamate 5-semialdehyde + NADP+ + H2O
L-glutamate + NADPH + H+
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
phenylpropionaldehyde + NAD+ + H2O
phenylpropionate + NADH + H+
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
-
-
?
succinic semialdehyde + NAD+ + H2O
succinate + NADH + H+
additional information
?
-
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
-
?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
-
?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
ir
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
ir
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
-
?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
-
ir
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
-
ir
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
-
ir
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
ir
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
-
?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
highly specific
-
ir
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
-
?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
-
?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
-
?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
-
?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
-
ir
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
-
?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
-
ir
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
-
?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
-
?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
-
?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
-
ir
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH + H+
-
-
-
?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH + H+
-
-
-
-
r
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH + H+
-
-
-
-
r
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH + H+
-
-
-
-
r
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH + H+
-
-
-
-
r
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH + H+
-
-
-
-
ir
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH + H+
-
-
-
?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH + H+
-
-
-
?
1-pyrroline-5-carboxylate + NADP+ + H2O
L-glutamate + NADPH + H+
-
-
-
-
r
1-pyrroline-5-carboxylate + NADP+ + H2O
L-glutamate + NADPH + H+
-
-
-
-
r
1-pyrroline-5-carboxylate + NADP+ + H2O
L-glutamate + NADPH + H+
-
-
-
-
r
1-pyrroline-5-carboxylate + NADP+ + H2O
L-glutamate + NADPH + H+
-
-
-
-
r
1-pyrroline-5-carboxylate + NADP+ + H2O
L-glutamate + NADPH + H+
-
NAD+ is preferred over NADP+
-
-
ir
2-aminoadipic semialdehyde + NAD+ + H2O
2-aminoadipate + NADH + H+
about 6% activity compared to L-glutamate 5-semialdehyde
-
-
?
2-aminoadipic semialdehyde + NAD+ + H2O
2-aminoadipate + NADH + H+
about 6% activity compared to L-glutamate 5-semialdehyde
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + H+
-
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + H+
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
about 5% activity compared to L-glutamate 5-semialdehyde
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
about 5% activity compared to L-glutamate 5-semialdehyde
-
-
?
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + H+
about 7.5% activity compared to L-glutamate 5-semialdehyde
-
-
?
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + H+
about 7.5% activity compared to L-glutamate 5-semialdehyde
-
-
?
DELTA1-pyrroline-3-hydroxy-5-carboxylate + NAD+ + H2O
4-hydroxyglutamate + NADH
-
-
-
?
DELTA1-pyrroline-3-hydroxy-5-carboxylate + NAD+ + H2O
4-hydroxyglutamate + NADH
-
-
-
-
?
glutaric semialdehyde + NAD+ + H2O
glutarate + NADH + H+
-
-
-
ir
glutaric semialdehyde + NAD+ + H2O
glutarate + NADH + H+
-
-
-
ir
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
-
two-electron oxidation in which a hydride is transferred toNAD+, producing NADH and glutamate
-
?
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
the bifunctional enzyme catalyzes the oxidation of proline in two steps. (S)-1-Pyrroline-5-carboxylate, the product of the first reaction is in spontaneous equilibrium with its tautomer L-glutamate gamma-semialdehyde: (1) L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor, (2) L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH + H+
-
-
?
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
-
-
-
ir
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
NAD+ is the preferred cofactor
-
-
ir
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
-
-
-
ir
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
-
-
-
ir
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
-
-
-
ir
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
NAD+ is the preferred cofactor
-
-
ir
L-glutamate 5-semialdehyde + NADP+ + H2O
L-glutamate + NADPH + H+
-
-
-
ir
L-glutamate 5-semialdehyde + NADP+ + H2O
L-glutamate + NADPH + H+
-
-
-
?
L-glutamate 5-semialdehyde + NADP+ + H2O
L-glutamate + NADPH + H+
-
-
-
?
L-glutamate 5-semialdehyde + NADP+ + H2O
L-glutamate + NADPH + H+
-
-
-
ir
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
about 5% activity compared to L-glutamate 5-semialdehyde
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
about 5% activity compared to L-glutamate 5-semialdehyde
-
-
?
phenylpropionaldehyde + NAD+ + H2O
phenylpropionate + NADH + H+
about 5% activity compared to L-glutamate 5-semialdehyde
-
-
?
phenylpropionaldehyde + NAD+ + H2O
phenylpropionate + NADH + H+
about 5% activity compared to L-glutamate 5-semialdehyde
-
-
?
succinic semialdehyde + NAD+ + H2O
succinate + NADH + H+
about 2% activity compared to L-glutamate 5-semialdehyde
-
-
?
succinic semialdehyde + NAD+ + H2O
succinate + NADH + H+
about 2% activity compared to L-glutamate 5-semialdehyde
-
-
?
additional information
?
-
-
enzyme involved in L-proline catabolism
-
-
?
additional information
?
-
-
enzyme involved in L-proline catabolism
-
-
?
additional information
?
-
-
not: pyrroline-2-carboxylate
-
-
?
additional information
?
-
kinetic model for the overall PRODH-P5CDH reaction of bifunctional PutA enzyme. The intermediate is not released into the bulk medium, but the mechanism follows substrate channeling. The rate of NADH formation is 20fold slower than the steady-state turnover number for the overall reaction, The limiting rate constant observed for NADH formation in the first turnover increases by almost 40fold after multiple turnovers, achieving half of the steady-state value after 15 turnovers
-
-
?
additional information
?
-
-
kinetic model for the overall PRODH-P5CDH reaction of bifunctional PutA enzyme. The intermediate is not released into the bulk medium, but the mechanism follows substrate channeling. The rate of NADH formation is 20fold slower than the steady-state turnover number for the overall reaction, The limiting rate constant observed for NADH formation in the first turnover increases by almost 40fold after multiple turnovers, achieving half of the steady-state value after 15 turnovers
-
-
?
additional information
?
-
-
slight activity with glutaric semialdehyde and adipic semialdehyde
-
-
?
additional information
?
-
enzyme involved in L-proline catabolism
-
-
?
additional information
?
-
-
enzyme involved in L-proline catabolism
-
-
?
additional information
?
-
-
additional esterase activity with p-nitrophenyl acetate as substrate, 50% of activity with 1-pyrroline-5-carboxylate, isoform A, only slight activity with isoform B
-
-
?
additional information
?
-
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
Q0DHN6
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
the enzyme shows a narrow substrate preference for L-glutamate 5-semialdehyde (GSAL) and glutaric semialdehyde (GRSAL)
-
-
-
additional information
?
-
-
the enzyme shows a narrow substrate preference for L-glutamate 5-semialdehyde (GSAL) and glutaric semialdehyde (GRSAL)
-
-
-
additional information
?
-
-
not: pyrroline-2-carboxylate
-
-
?
additional information
?
-
-
not: glyceraldehyde, valeraldehyde
-
-
?
additional information
?
-
-
slight activity with glutaric semialdehyde and adipic semialdehyde
-
-
?
additional information
?
-
-
not: pyrroline-2-carboxylate
-
-
?
additional information
?
-
-
enzyme involved in L-proline catabolism
-
-
?
additional information
?
-
-
enzyme with 2 activities: proline oxidase and 1-pyrroline-5-carboxylate dehydrogenase, which require different reaction conditions
-
-
?
additional information
?
-
-
enzyme with 2 activities: proline oxidase and 1-pyrroline-5-carboxylate dehydrogenase, which require different reaction conditions
-
-
?
additional information
?
-
-
catalyzes last step in both arginine and proline catabolism
-
-
?
additional information
?
-
-
no reverse reaction using L-glutamate as substrate within pH 5.5 to pH 10.0
-
-
?
additional information
?
-
-
not: pyrroline-2-carboxylate
-
-
?
additional information
?
-
the enzyme shows a narrow substrate preference for L-glutamate 5-semialdehyde (GSAL) and glutaric semialdehyde (GRSAL)
-
-
-
additional information
?
-
-
the enzyme shows a narrow substrate preference for L-glutamate 5-semialdehyde (GSAL) and glutaric semialdehyde (GRSAL)
-
-
-
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0.037 - 2
1-pyrroline-5-carboxylate
0.173 - 0.211
2-aminoadipic semialdehyde
0.5
3-Methoxybenzaldehyde
-
isoform A
0.25
4-methoxybenzaldehyde
-
isoform A
1
acetaldehyde
-
isoform A
0.5
benzaldehyde
-
isoform A
0.133
D-glucose
-
isoform A
1.86
D-glyceraldehyde 3-phosphate
pH 7.5, 30°C, recombinant wild-type enzyme
0.76
formaldehyde
-
isoform A
0.032 - 0.48
Glutaric semialdehyde
1
glyoxylic acid
-
isoform A
0.2
indol-3-acetaldehyde
-
isoform A
0.12 - 97
L-glutamate 5-semialdehyde
0.27
p-nitrobenzaldehyde
-
isoform A
additional information
additional information
-
0.037
1-pyrroline-5-carboxylate
-
pH 7.4, 50°C
0.062
1-pyrroline-5-carboxylate
-
with NADP+
0.09
1-pyrroline-5-carboxylate
-
-
0.104
1-pyrroline-5-carboxylate
pH 7.5, 20°C
0.109
1-pyrroline-5-carboxylate
-
-
0.17
1-pyrroline-5-carboxylate
-
-
0.18
1-pyrroline-5-carboxylate
-
-
0.2
1-pyrroline-5-carboxylate
-
isoform B, with NADP+
0.265
1-pyrroline-5-carboxylate
-
cosubstrate NADP+, pH 7.5, 35°C
0.29
1-pyrroline-5-carboxylate
-
with NAD+
0.3
1-pyrroline-5-carboxylate
-
isoform B, with NAD+
0.3
1-pyrroline-5-carboxylate
-
isoform A, with NADP+
0.33
1-pyrroline-5-carboxylate
-
isoform A, with NAD+
0.35
1-pyrroline-5-carboxylate
-
-
0.358
1-pyrroline-5-carboxylate
-
cosubstrate NAD+, pH 7.5, 35°C
0.42
1-pyrroline-5-carboxylate
-
isoform I
0.42
1-pyrroline-5-carboxylate
-
with NADP+
0.46
1-pyrroline-5-carboxylate
-
-
0.75
1-pyrroline-5-carboxylate
-
with NAD+
1.22
1-pyrroline-5-carboxylate
-
isoform II
2
1-pyrroline-5-carboxylate
pH 7.5, 21°C
0.173
2-aminoadipic semialdehyde
pH 7.5, 30°C, recombinant wild-type enzyme
0.211
2-aminoadipic semialdehyde
pH 7.5, 30°C, recombinant wild-type enzyme
0.032
Glutaric semialdehyde
pH 7.5, 30°C, recombinant mutant E205A
0.082
Glutaric semialdehyde
pH 7.5, 30°C, recombinant wild-type enzyme
0.084
Glutaric semialdehyde
pH 7.5, 30°C, recombinant wild-type enzyme
0.227
Glutaric semialdehyde
pH 7.5, 30°C, recombinant mutant S331A
0.379
Glutaric semialdehyde
pH 7.5, 30°C, recombinant mutant F505A
0.442
Glutaric semialdehyde
pH 7.5, 30°C, recombinant mutant K329A
0.48
Glutaric semialdehyde
pH 7.5, 30°C, recombinant mutant F202A
0.12
L-glutamate 5-semialdehyde
pH 7.5, 30°C, recombinant mutant E205A
0.17
L-glutamate 5-semialdehyde
pH 7.5, 30°C, recombinant mutant F505A
0.198
L-glutamate 5-semialdehyde
pH 7.5, 30°C, recombinant wild-type enzyme
0.228
L-glutamate 5-semialdehyde
pH 7.5, 30°C, recombinant wild-type enzyme
0.266
L-glutamate 5-semialdehyde
pH 7.5, 30°C, recombinant mutant D226A
0.624
L-glutamate 5-semialdehyde
pH 7.5, 30°C, recombinant mutant S331A
0.958
L-glutamate 5-semialdehyde
pH 7.5, 30°C, recombinant mutant K329A
0.969
L-glutamate 5-semialdehyde
pH 7.5, 30°C, recombinant mutant F202A
97
L-glutamate 5-semialdehyde
pH 7.2, 28°C
0.02
NAD+
-
isoform I
0.0235
NAD+
overall reaction of bifunctional enzyme, pH 7.5, 21°C
0.071
NAD+
-
pH 7.4, 50°C
0.119
NAD+
pH 7.5, 30°C, recombinant mutant D226A
0.185
NAD+
pH 7.5, 30°C, recombinant wild-type enzyme
0.227
NAD+
pH 7.5, 30°C, recombinant wild-type enzyme
0.644
NAD+
-
pH 7.5, 35°C
4.695
NAD+
-
pH 7.5, 35°C
0.0095
NADP+
-
-
0.071
NADP+
pH 7.5, 30°C, recombinant mutant D226A
0.12
NADP+
-
pH 7.4, 50°C
2.872
NADP+
pH 7.5, 30°C, recombinant wild-type enzyme
3.066
NADP+
pH 7.5, 30°C, recombinant wild-type enzyme
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.5 - 25
1-pyrroline-5-carboxylate
0.005 - 0.04
2-aminoadipic semialdehyde
0.4
D-glyceraldehyde 3-phosphate
pH 7.5, 30°C, recombinant wild-type enzyme
0.21 - 1.9
Glutaric semialdehyde
0.03 - 7
L-glutamate 5-semialdehyde
1.5
1-pyrroline-5-carboxylate
pH 7.5, 20°C
1.6
1-pyrroline-5-carboxylate
-
pH 7.4, 50°C
5.16
1-pyrroline-5-carboxylate
pH 7.5, 21°C
25
1-pyrroline-5-carboxylate
-
-
0.005
2-aminoadipic semialdehyde
pH 7.5, 30°C, recombinant wild-type enzyme
0.04
2-aminoadipic semialdehyde
pH 7.5, 30°C, recombinant wild-type enzyme
0.21
Glutaric semialdehyde
pH 7.5, 30°C, recombinant mutant F202A
0.3
Glutaric semialdehyde
pH 7.5, 30°C, recombinant wild-type enzyme
0.31
Glutaric semialdehyde
pH 7.5, 30°C, recombinant mutant K329A
0.52
Glutaric semialdehyde
pH 7.5, 30°C, recombinant mutant F505A
0.53
Glutaric semialdehyde
pH 7.5, 30°C, recombinant mutant E205A
0.89
Glutaric semialdehyde
pH 7.5, 30°C, recombinant mutant S331A
1.9
Glutaric semialdehyde
pH 7.5, 30°C, recombinant wild-type enzyme
0.03
L-glutamate 5-semialdehyde
pH 7.5, 30°C, recombinant mutant F505A
0.15
L-glutamate 5-semialdehyde
pH 7.5, 30°C, recombinant mutant F202A
0.21
L-glutamate 5-semialdehyde
pH 7.5, 30°C, recombinant mutant E205A
0.26
L-glutamate 5-semialdehyde
pH 7.5, 30°C, recombinant mutant K329A
0.44
L-glutamate 5-semialdehyde
pH 7.5, 30°C, recombinant wild-type enzyme
1.83
L-glutamate 5-semialdehyde
pH 7.5, 30°C, recombinant mutant S331A
3.6
L-glutamate 5-semialdehyde
pH 7.5, 30°C, recombinant mutant D226A
6.8
L-glutamate 5-semialdehyde
pH 7.5, 30°C, recombinant wild-type enzyme
7
L-glutamate 5-semialdehyde
pH 7.2, 28°C
0.17
NAD+
pH 7.5, 30°C, recombinant wild-type enzyme
1.7
NAD+
pH 7.5, 30°C, recombinant mutant D226A
3.1
NAD+
pH 7.5, 30°C, recombinant wild-type enzyme
0.05
NADP+
pH 7.5, 30°C, recombinant wild-type enzyme
0.42
NADP+
-
pH 7.4, 50°C
0.8
NADP+
pH 7.5, 30°C, recombinant wild-type enzyme
1.5
NADP+
pH 7.5, 30°C, recombinant mutant D226A
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E314A
inactive. The conserved Glu447 residue has significantly shifted in the mutant, causing NAD+ to be displaced
S352A
catalytic site including the oxoanion hole and residue Cys348 remain unchanged in the mutant, and the coenzyme maintains its binding position
S352L
inactive. The conserved Glu447 residue has significantly shifted in the mutant, causing NAD+ to be displaced
W193A
mutation disrupts hexamer formation, mutant forms a dimer
K104A
mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, mutant forms a hexamer
R100A
mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, contrary to wild-type, the mutant forms a dimer
R100A/K104A/R111A
mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, contrary to wild-type, the mutant forms a dimer
R111A
mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, mutant forms a hexamer
R153A
mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, mutant forms a hexamer
K104A
-
mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, mutant forms a hexamer
-
R100A
-
mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, contrary to wild-type, the mutant forms a dimer
-
R100A/K104A/R111A
-
mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, contrary to wild-type, the mutant forms a dimer
-
R111A
-
mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, mutant forms a hexamer
-
R153A
-
mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, mutant forms a hexamer
-
C330A
site-directed mutagenesis, inactive mutant
D226A
site-directed mutagenesis, the mutant shows altered kinetics compared to wild-type enzyme
E205A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
F202A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
F505A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
K329A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
P86S/V88M/A127T/V468I/V532I
the maize cultivar Cellux cDNA sequence differs in 15 bases leading to five amino acid substitutions compared to the sequenced B73 cultivar, UniProt ID A0A2H4PMI3
S331A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
R102A
mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, contrary to wild-type, the mutant forms a dimer
R102A
-
mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, contrary to wild-type, the mutant forms a dimer
-
additional information
impairment of pyrroline-5-carboxylate oxidation in the p5cdh mutant does not change the cellular Pro to P5C ratio under ambient and osmotic stress conditions. Lack of P5CDH activity leads to higher ROS production under dark and light conditions in the presence of Pro excess, as well as renders plants hypersensitive to heat stress
additional information
-
mutant strain MB2281-10C with deficiency in enzyme
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