EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.1.1.95 | H447A | site-directed mutagenesis, the mutant shows altered L-serine binding, kinetics for NADH, and activity compared to the wild-type enzyme | Mycobacterium tuberculosis |
1.1.1.95 | K439A | site-directed mutagenesis, the mutant shows altered L-serine binding, kinetics for NADH, and activity compared to the wild-type enzyme | Mycobacterium tuberculosis |
1.1.1.95 | K439A/R451A/R501A | site-directed mutagenesis, the mutation eliminates substrate inhibition and pH-dependent depression in activity | Mycobacterium tuberculosis |
1.1.1.95 | R446A | site-directed mutagenesis, the mutant shows altered L-serine binding, kinetics for NADH, and activity compared to the wild-type enzyme | Mycobacterium tuberculosis |
1.1.1.95 | R451A | site-directed mutagenesis, the mutant shows altered L-serine binding, kinetics for NADH, and activity compared to the wild-type enzyme | Mycobacterium tuberculosis |
1.1.1.95 | R451A/R501A/K439A | site-directed mutagenesis, the mutation eliminates substrate inhibition and pH-dependent depression in activity | Mycobacterium tuberculosis |
1.1.1.95 | R501A | site-directed mutagenesis, the mutant shows altered L-serine binding, kinetics for NADH, and activity compared to the wild-type enzyme | Mycobacterium tuberculosis |
1.1.1.95 | W130F | site-directed mutagenesis, catalytically inactive mutant | Mycobacterium tuberculosis |
1.1.1.95 | W29F | site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme | Mycobacterium tuberculosis |
1.1.1.95 | W327F | site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme | Mycobacterium tuberculosis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.95 | L-serine | two serine molecules bound to the regulatory domain, anion- and serine-binding sites between two adjacent subunits | Mycobacterium tuberculosis | |
1.1.1.95 | additional information | mechanism of substrate inhibition, linked to this pH-dependent depression in activity, overview | Mycobacterium tuberculosis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.95 | additional information | - |
additional information | kinetic analysis of wild-type and mutant enzymes | 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 | 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+ | catalytic His280, active site, regulatory, and substrate binding site structures, overview | Mycobacterium tuberculosis | ? | - |
? | |
1.1.1.95 | phosphonooxypyruvate + NADH + H+ | - |
Mycobacterium tuberculosis H37Rv | ? | - |
? | |
1.1.1.95 | phosphonooxypyruvate + NADH + H+ | catalytic His280, active site, regulatory, and substrate binding site structures, overview | Mycobacterium tuberculosis H37Rv | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.1.1.95 | tetramer | intervening domains are the two four-stranded beta-sheet structures located next to the substrate binding domains and below the regulatory domains, structure model, overview | Mycobacterium tuberculosis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.1.1.95 | 25 | - |
assay at | 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 | nucleotide binding site structure, overview | Mycobacterium tuberculosis |