1.2.1.88: L-glutamate gamma-semialdehyde dehydrogenase
This is an abbreviated version!
For detailed information about L-glutamate gamma-semialdehyde dehydrogenase, go to the full flat file.
Word Map on EC 1.2.1.88
Reaction
Synonyms
1-pyrroline dehydrogenase, aldehyde dehydrogenase 12, ALDH12, Aldh4a1, dehydrogenase, 1-pyrroline-5-carboxylate, DELTA1-pyrroline-5-carboxylate dehydrogenase, delta1-pyrroline-5-carboxylate synthetase, DR_0813, EC 1.5.1.12, GSAL dehydrogenase, GSALDH, l-glutamate-gamma-semialdehyde dehydrogenase, L-pyrroline-5-carboxylate-NAD+ oxidoreductase, LRRP Ba1-651, NAD+-dependent glutamate gamma-semialdehyde dehydrogenase, OsALDH12, OsALDH18-2, P5C dehydrogenase, P5C synthase, P5C-DH, P5CD, P5CDH, P5CDH1, P5CS, PDH, PpALDH12, proline/P5C dehydrogenase, Put2, PutA, pyrroline-5-carboxylate dehydrogenase, pyrroline-5-carboxylate synthase, pyrroline-5-carboxylic acid dehydrogenase, Tc00.1047053510943.50, YcgN, ZmALDH12
ECTree
1.2.1.88 L-glutamate gamma-semialdehyde dehydrogenaseAdvanced search results
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results (Engineering
Engineering on EC 1.2.1.88 - L-glutamate gamma-semialdehyde dehydrogenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
R102A
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
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, mutant forms a hexamer
-
R100A
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
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
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
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
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, mutant forms a hexamer
-
R153A
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, mutant forms a hexamer
-
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
additional information
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
