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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
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mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, mutant forms a hexamer
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R100A
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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
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R100A/K104A/R111A
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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
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R111A
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mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, mutant forms a hexamer
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R153A
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mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, mutant forms a hexamer
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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
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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
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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
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mutant strain MB2281-10C with deficiency in enzyme