EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.1.95 | expression of tagged wild-type and mutant enzymes | Mycobacterium tuberculosis |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.1.1.95 | D-3-phosphoglycerate dehydrogenase with bound effector L-serine or with bound substrate hydroxypyruvic acid phosphate, PGDH at 10 mg/ml is mixed with 5 mM hydroxypyruvic acid phosphate and 5 mM NAD+ analogue 3-acetyl pyridine adenine dinucleotide, or with 5 mM NADH and 5 mM L-serine, from 1 M Na K tartrate, 0.1 M MES, pH 6.5, cryoprotection in 25% propylene glycol, X-ray diffraction structure determination and analysis at resolutions of 2.7 A and 2.4 A, respectively | Mycobacterium tuberculosis |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.1.1.95 | D463A | site-directed mutagenesis, a very large reduction in the sensitivity of the mutant enzyme to L-serine | Mycobacterium tuberculosis |
1.1.1.95 | G316V | site-directed mutagenesis, the mutant shows slightly reduced activity and decreased sensitivity to L-serine compared to the wild-type | Mycobacterium tuberculosis |
1.1.1.95 | G316V/G317V | site-directed mutagenesis, the mutant shows reduced activity and decreased sensitivity to L-serine compared to the wild-type | Mycobacterium tuberculosis |
1.1.1.95 | G316V/G317V/G318V | site-directed mutagenesis, the mutant is not producable | Mycobacterium tuberculosis |
1.1.1.95 | G316V/G318V | site-directed mutagenesis, the mutant shows reduced activity and decreased sensitivity to L-serine compared to the wild-type | Mycobacterium tuberculosis |
1.1.1.95 | G317V | site-directed mutagenesis, the mutant shows slightly reduced activity and decreased sensitivity to L-serine compared to the wild-type | Mycobacterium tuberculosis |
1.1.1.95 | G317V/G318V | site-directed mutagenesis, the mutant shows reduced activity and decreased sensitivity to L-serine compared to the wild-type | Mycobacterium tuberculosis |
1.1.1.95 | G318V | site-directed mutagenesis, the mutant shows slightly reduced activity and decreased sensitivity to L-serine compared to the wild-type | Mycobacterium tuberculosis |
1.1.1.95 | 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 | Mycobacterium tuberculosis |
1.1.1.95 | Y461A | site-directed mutagenesis, a very large reduction in the sensitivity of the mutant enzyme to L-serine | Mycobacterium tuberculosis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.95 | L-serine | - |
Mycobacterium tuberculosis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.95 | additional information | - |
additional information | stopped flow and steady-state kinetic analysis | Mycobacterium tuberculosis | |
1.1.1.95 | 0.114 | - |
NADH | pH 7.5, 25°C, recombinant mutant G316V | Mycobacterium tuberculosis | |
1.1.1.95 | 0.12 | - |
NADH | pH 7.5, 25°C, recombinant mutant N481A | Mycobacterium tuberculosis | |
1.1.1.95 | 0.14 | - |
NADH | pH 7.5, 25°C, recombinant mutant D463A | Mycobacterium tuberculosis | |
1.1.1.95 | 0.165 | - |
NADH | pH 7.5, 25°C, recombinant mutant G317V | Mycobacterium tuberculosis | |
1.1.1.95 | 0.17 | - |
NADH | pH 7.5, 25°C, wild-type enzyme | Mycobacterium tuberculosis | |
1.1.1.95 | 0.203 | - |
NADH | pH 7.5, 25°C, recombinant mutant G318V | Mycobacterium tuberculosis | |
1.1.1.95 | 0.22 | - |
NADH | pH 7.5, 25°C, recombinant mutant G317V/G318V | Mycobacterium tuberculosis | |
1.1.1.95 | 0.27 | - |
NADH | pH 7.5, 25°C, recombinant mutant Y461A | Mycobacterium tuberculosis | |
1.1.1.95 | 0.47 | - |
NADH | pH 7.5, 25°C, recombinant mutant G316V/G318V | Mycobacterium tuberculosis | |
1.1.1.95 | 0.61 | - |
NADH | pH 7.5, 25°C, recombinant mutant G316V/G317V | Mycobacterium tuberculosis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.95 | phosphonooxypyruvate + NADH + H+ | Mycobacterium tuberculosis | - |
? | - |
? | |
1.1.1.95 | phosphonooxypyruvate + NADH + H+ | Mycobacterium tuberculosis H37Rv | - |
? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.95 | Mycobacterium tuberculosis | P9WNX3 | - |
- |
1.1.1.95 | Mycobacterium tuberculosis H37Rv | P9WNX3 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.1.1.95 | recombinant tagged wild-type and mutant enzymes | Mycobacterium tuberculosis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.95 | phosphonooxypyruvate + NADH + H+ | - |
Mycobacterium tuberculosis | ? | - |
? | |
1.1.1.95 | phosphonooxypyruvate + NADH + H+ | very slow NADH binding in absence of substrate, productive NADH binding, that would support catalytic turnover, is dependent on the presence of substrate, active site structure with the catalytic His280, modelling of ligand-free and substrate-bound active site, overview | Mycobacterium tuberculosis | ? | - |
? | |
1.1.1.95 | phosphonooxypyruvate + NADH + H+ | - |
Mycobacterium tuberculosis H37Rv | ? | - |
? | |
1.1.1.95 | phosphonooxypyruvate + NADH + H+ | very slow NADH binding in absence of substrate, productive NADH binding, that would support catalytic turnover, is dependent on the presence of substrate, active site structure with the catalytic His280, modelling of ligand-free and substrate-bound active site, overview | Mycobacterium tuberculosis H37Rv | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.1.1.95 | More | the apo-enzyme shows an extreme asymmetry in the orientation of the domains from one subunit to another. The poly glycine stretch in the loop that contains the locus for the 160° rotation leads to subunit asymmetry, structure modelling, overview | Mycobacterium tuberculosis |
1.1.1.95 | tetramer | ligand-bound enzyme, sequence comparison | Mycobacterium tuberculosis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.95 | D-3-phosphoglycerate dehydrogenase | - |
Mycobacterium tuberculosis |
1.1.1.95 | PGDH | - |
Mycobacterium tuberculosis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.1.1.95 | 25 | - |
assay at | Mycobacterium tuberculosis |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.95 | 603 | - |
NADH | pH 7.5, 25°C, recombinant mutant N481A | Mycobacterium tuberculosis | |
1.1.1.95 | 605 | - |
NADH | pH 7.5, 25°C, recombinant mutant G317V/G318V | Mycobacterium tuberculosis | |
1.1.1.95 | 720 | - |
NADH | pH 7.5, 25°C, recombinant mutant D463A | Mycobacterium tuberculosis | |
1.1.1.95 | 1111 | - |
NADH | pH 7.5, 25°C, recombinant mutant G316V | Mycobacterium tuberculosis | |
1.1.1.95 | 2111 | - |
NADH | pH 7.5, 25°C, recombinant mutant G317V | Mycobacterium tuberculosis | |
1.1.1.95 | 2349 | - |
NADH | pH 7.5, 25°C, recombinant mutant G318V | Mycobacterium tuberculosis | |
1.1.1.95 | 2461 | - |
NADH | pH 7.5, 25°C, wild-type enzyme | Mycobacterium tuberculosis | |
1.1.1.95 | 2754 | - |
NADH | pH 7.5, 25°C, recombinant mutant Y461A | Mycobacterium tuberculosis | |
1.1.1.95 | 2805 | - |
NADH | pH 7.5, 25°C, recombinant mutant G316V/G317V | Mycobacterium tuberculosis | |
1.1.1.95 | 2827 | - |
NADH | pH 7.5, 25°C, recombinant mutant G316V/G318V | Mycobacterium tuberculosis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.95 | 7.5 | - |
assay at | Mycobacterium tuberculosis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.95 | NADH | cofactor binding site structure and binding mechanism, overview | Mycobacterium tuberculosis |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.95 | 0.22 | - |
L-serine | pH 7.5, 25°C, recombinant mutant G316V/G318V | Mycobacterium tuberculosis | |
1.1.1.95 | 0.38 | - |
L-serine | pH 7.5, 25°C, recombinant mutant G316V/G317V | Mycobacterium tuberculosis | |
1.1.1.95 | 0.42 | - |
L-serine | pH 7.5, 25°C, recombinant mutant Y461A | Mycobacterium tuberculosis | |
1.1.1.95 | 0.95 | - |
L-serine | pH 7.5, 25°C, wild-type enzyme | Mycobacterium tuberculosis | |
1.1.1.95 | 1.09 | - |
L-serine | pH 7.5, 25°C, recombinant mutant D463A | Mycobacterium tuberculosis | |
1.1.1.95 | 1.11 | - |
L-serine | pH 7.5, 25°C, recombinant mutant G317V | Mycobacterium tuberculosis | |
1.1.1.95 | 1.62 | - |
L-serine | pH 7.5, 25°C, recombinant mutant G317V/G318V | Mycobacterium tuberculosis | |
1.1.1.95 | 1.925 | - |
L-serine | pH 7.5, 25°C, recombinant mutant G318V | Mycobacterium tuberculosis | |
1.1.1.95 | 2.231 | - |
L-serine | pH 7.5, 25°C, recombinant mutant G316V | Mycobacterium tuberculosis | |
1.1.1.95 | 2.32 | - |
L-serine | pH 7.5, 25°C, recombinant mutant N481A | Mycobacterium tuberculosis |