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Literature summary for 1.1.1.95 extracted from

  • Burton, R.L.; Chen, S.; Xu, X.L.; Grant, G.A.
    Role of the anion-binding site in catalysis and regulation of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase (2009), Biochemistry, 48, 4808-4815.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.95

Protein Variants

Protein Variants Comment Organism
H447A site-directed mutagenesis, the mutant shows altered L-serine binding, kinetics for NADH, and activity compared to the wild-type enzyme Mycobacterium tuberculosis
K439A site-directed mutagenesis, the mutant shows altered L-serine binding, kinetics for NADH, and activity compared to the wild-type enzyme Mycobacterium tuberculosis
K439A/R451A/R501A site-directed mutagenesis, the mutation eliminates substrate inhibition and pH-dependent depression in activity Mycobacterium tuberculosis
R446A site-directed mutagenesis, the mutant shows altered L-serine binding, kinetics for NADH, and activity compared to the wild-type enzyme Mycobacterium tuberculosis
R451A site-directed mutagenesis, the mutant shows altered L-serine binding, kinetics for NADH, and activity compared to the wild-type enzyme Mycobacterium tuberculosis
R451A/R501A/K439A site-directed mutagenesis, the mutation eliminates substrate inhibition and pH-dependent depression in activity Mycobacterium tuberculosis
R501A site-directed mutagenesis, the mutant shows altered L-serine binding, kinetics for NADH, and activity compared to the wild-type enzyme Mycobacterium tuberculosis
W130F site-directed mutagenesis, catalytically inactive mutant Mycobacterium tuberculosis
W29F site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Mycobacterium tuberculosis
W327F site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
L-serine two serine molecules bound to the regulatory domain, anion- and serine-binding sites between two adjacent subunits Mycobacterium tuberculosis
additional information mechanism of substrate inhibition, linked to this pH-dependent depression in activity, overview Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic analysis of wild-type and mutant enzymes Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
phosphonooxypyruvate + NADH + H+ Mycobacterium tuberculosis
-
 ?
-
 ?
phosphonooxypyruvate + NADH + H+ Mycobacterium tuberculosis H37Rv
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WNX3
-
-
Mycobacterium tuberculosis H37Rv P9WNX3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphonooxypyruvate + NADH + H+
-
 Mycobacterium tuberculosis ?
-
 ?
phosphonooxypyruvate + NADH + H+ catalytic His280, active site, regulatory, and substrate binding site structures, overview Mycobacterium tuberculosis ?
-
 ?
phosphonooxypyruvate + NADH + H+
-
 Mycobacterium tuberculosis H37Rv ?
-
 ?
phosphonooxypyruvate + NADH + H+ catalytic His280, active site, regulatory, and substrate binding site structures, overview Mycobacterium tuberculosis H37Rv ?
-
 ?

Subunits

Subunits Comment Organism
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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
NADH nucleotide binding site structure, overview Mycobacterium tuberculosis