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1.1.1.95: phosphoglycerate dehydrogenase

This is an abbreviated version!
For detailed information about phosphoglycerate dehydrogenase, go to the full flat file.

Word Map on EC 1.1.1.95

Reaction

3-phospho-D-glycerate
+
NAD+
=
3-phosphooxypyruvate
 +
NADH
 +
H+

Synonyms

3-PGDH, 3-phosphoglycerate dehydrogenase, 3-phosphoglyceric acid dehydrogenase, 3PGDH, A10, alpha-phosphoglycerate dehydrogenase, ApPGDH, At1g17745, At3g19480, At4g34200, BvSHMTa, BvSHMTb, D-3-PG dehydrogenase, D-3-phosphoglycerate dehydrogenase, D-3-phosphoglycerate:NAD oxidoreductase, D-phosphoglycerate dehydrogenase, dehydrogenase, phosphoglycerate, EDA9, EhPGDH, glycerate 3-phosphate dehydrogenase, glycerate-1,3-phosphate dehydrogenase, MARPO_0030s0029, More, NAD-dependent D-3-phosphoglycerate dehydrogenase, PGDH, PGDH1, PGDH2, PGDH3, PGK, Phgdh, phosphoglycerate dehydrogenase, phosphoglycerate kinase, phosphoglycerate oxidoreductase, phosphoglyceric acid dehydrogenase, Rv2996c, serA, serA1, type 1 D-3-phosphoglycerate dehydrogenase, type III 3-phosphoglycerate dehydrogenase, type IIIK PGDH

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.95 phosphoglycerate dehydrogenase

Engineering

Engineering on EC 1.1.1.95 - phosphoglycerate dehydrogenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E108A
-
in contrast to wild-type mutant existed as monomer even at pH 7
K263A
the mutant shows strongly reduced activity compared to the wild type enzyme
A143A
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
A144V
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
A374V
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
D317A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
D386A
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
E299A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
E302A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
E307A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
E345A
site-directed mutagenesis, mutation of a residue in the serine binding site, the mutant shows only slightly altered kinetics and activity compared to the wild-type enzyme
E360A
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
E387A
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
G145V
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
G336V
G336V/G337V
changing glycine residues 336 and 337 to valine affect the sensitivity of the enzyme to inhibition by L-serine but not the extent of inhibition. The decrease in sensitivity is caused primarily by a decrease in the affinity of the enzyme for L-serine. The mutations also affect the domain rotation of the subunits in response to L-serine binding
G337V
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
G349V
site-directed mutagenesis, mutation of a residue in the serine binding site, the mutant shows only slightly altered kinetics and activity compared to the wild-type enzyme
G362V
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
H335A
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
H344A
H344A/N364A
-
no inhibition by L-serine
K141A
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
K141R
kcat/KM for 2-oxoglutarate is 4.8fold lower than the value for the wild-type enzyme, kcat/KM for 3-phosphooxypyruvate is 2.6fold higher than the value for the wild-type enzyme
K311A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
N190A
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, no protein expression
N303A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
N303A/K311A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
N346A
N346A/H344A
-
no inhibition by L-serine
N346A/N364A
-
no inhibition by L-serine
N364A
P348A
site-directed mutagenesis, mutation of a residue in the serine binding site, the mutant shows only slightly altered kinetics and activity compared to the wild-type enzyme
Q298A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
Q301A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
Q361A
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
Q375A
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
R338A
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
R347A
site-directed mutagenesis, mutation of a residue in the serine binding site, the mutant shows only slightly altered kinetics and activity compared to the wild-type enzyme
S107A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
S107A/S111A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
S111A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
S111A/K311A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
S296A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
S316A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
S323A
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
S373A
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
T297A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
W139F/E360W
exhibits catalytic activity comparable to that of the native enzyme and is effectively inhibited by L-serine. The only fluorescence signal of the mutant is due to the single tryptophan at position 360. Pre-steady state analysis of binding of inhibitor serine shows that each serine binding interface produces an integrated fluorescent signal
W139F/E360W/G294V
-
placement of a tryptophanyl residue near the serine binding site (W139F/E360W) allows serine binding to be monitored by fluorescence quenching analysis. Pre-steady state analysis demonstrate that serine binds to two forms of the free enzyme, E and E*. Conversion of Gly-336 to valine has its main effect on the Kd of serine binding to one form of the free enzyme (E) while maintaining the cooperativity of binding observed in the native enzyme
W139F/E360W/G336V
-
placement of a tryptophanyl residue near the serine binding site (W139F/E360W) allows serine binding to be monitored by fluorescence quenching analysis. Pre-steady state analysis demonstrate that serine binds to two forms of the free enzyme, E and E*. Conversion of Gly-294 to valine eliminates a rate limiting conformational change that follows serine binding to E. The conformational change between the two forms of free enzyme is maintained, but the Hill coefficient for cooperativity is significantly lowered
K141R
-
kcat/KM for 2-oxoglutarate is 4.8fold lower than the value for the wild-type enzyme, kcat/KM for 3-phosphooxypyruvate is 2.6fold higher than the value for the wild-type enzyme
-
A373T
naturally occuring mutation located in the nucleotide binding and regulatory domains of 3-PGDH, the mutation does not affect steady-state expression, protein stability, and protein degradation rates, the mutant is almost catalytically inactive
G377S
naturally occuring mutation located in the nucleotide binding and regulatory domains of 3-PGDH, the mutation does not affect steady-state expression, protein stability, and protein degradation rates, the mutant is almost catalytically inactive
R135W
naturally occuring mutation located in the nucleotide binding and regulatory domains of 3-PGDH, the mutation does not affect steady-state expression, protein stability, and protein degradation rates, the mutant is almost catalytically inactive
V261M
naturally occuring mutation located in the nucleotide binding and regulatory domains of 3-PGDH, the mutation does not affect steady-state expression, protein stability, and protein degradation rates, the mutant is almost catalytically inactive
V425M
naturally occuring mutation in the carboxy-terminal regulatory domain, leads to 3-PGDH deficiency, the mutant is almost catalytically inactive
V490M
naturally occuring mutation in the carboxy-terminal regulatory domain, leads to 3-PGDH deficiency, the mutant is almost catalytically inactive
up
-
Phgdh is transiently upregulated in the brain by kainic acid-treatment, causing selective lesions in the hippocampal region, kainic acid is injected into the bregma, overview
D463A
site-directed mutagenesis, a very large reduction in the sensitivity of the mutant enzyme to L-serine
G316V
site-directed mutagenesis, the mutant shows slightly reduced activity and decreased sensitivity to L-serine compared to the wild-type
G316V/G317V
site-directed mutagenesis, the mutant shows reduced activity and decreased sensitivity to L-serine compared to the wild-type
G316V/G317V/G318V
site-directed mutagenesis, the mutant is not producable
G316V/G318V
site-directed mutagenesis, the mutant shows reduced activity and decreased sensitivity to L-serine compared to the wild-type
G317V
site-directed mutagenesis, the mutant shows slightly reduced activity and decreased sensitivity to L-serine compared to the wild-type
G317V/G318V
site-directed mutagenesis, the mutant shows reduced activity and decreased sensitivity to L-serine compared to the wild-type
G318V
site-directed mutagenesis, the mutant shows slightly reduced activity and decreased sensitivity to L-serine compared to the wild-type
H447A
K439A
K439A/R451A/R501A
site-directed mutagenesis, the mutation eliminates substrate inhibition and pH-dependent depression in activity
N481A
site-directed mutagenesis, a very large reduction in the sensitivity of the mutant enzyme to L-serine. Mutant N481A co-elutes with native PGDH in gel filtration, it shows loss of cooperativity, which cannot be explained by a change in the quaternary structure of the enzyme from tetramer to dimer or monomer
R132K
mutation decreases the Km-value for 3-phosphooxypyruvate by approximately 10fold
R446A
R451A
R451A/R501A/K439A
site-directed mutagenesis, the mutation eliminates substrate inhibition and pH-dependent depression in activity
R501A
R501A/R451A/K439A
anion binding site mutant: Km (mM) (3-phosphohydroxypyruvate): 0.243, kcat: 1558, Ki (mM) (3-phosphohydroxypyruvate): 7.218, mutant displays only little uncompetitive substrate inhibition, no dual pH optima compared to wild-type
R72A
mutant enzyme utilize 2-oxoglutarate as substrate
R72L
mutant enzyme utilize 2-oxoglutarate as substrate
W130F
site-directed mutagenesis, catalytically inactive mutant
W29F
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
W327F
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y461A
site-directed mutagenesis, a very large reduction in the sensitivity of the mutant enzyme to L-serine
D463A
-
site-directed mutagenesis, a very large reduction in the sensitivity of the mutant enzyme to L-serine
-
G316V
-
site-directed mutagenesis, the mutant shows slightly reduced activity and decreased sensitivity to L-serine compared to the wild-type
-
G316V/G317V/G318V
-
site-directed mutagenesis, the mutant is not producable
-
H447A
K439A
N481A
-
site-directed mutagenesis, a very large reduction in the sensitivity of the mutant enzyme to L-serine. Mutant N481A co-elutes with native PGDH in gel filtration, it shows loss of cooperativity, which cannot be explained by a change in the quaternary structure of the enzyme from tetramer to dimer or monomer
-
R132K
-
mutation decreases the Km-value for 3-phosphooxypyruvate by approximately 10fold
-
R446A
R451A
R501A
R72A
-
mutant enzyme utilize 2-oxoglutarate as substrate
-
R72L
-
mutant enzyme utilize 2-oxoglutarate as substrate
-
Y461A
-
site-directed mutagenesis, a very large reduction in the sensitivity of the mutant enzyme to L-serine
-
additional information